Advances and prospects in microbial production of biotin.
Biosynthetic pathway
Biotin
Chemical mutagenesis
Metabolic engineering
Journal
Microbial cell factories
ISSN: 1475-2859
Titre abrégé: Microb Cell Fact
Pays: England
ID NLM: 101139812
Informations de publication
Date de publication:
12 May 2024
12 May 2024
Historique:
received:
25
01
2024
accepted:
30
04
2024
medline:
13
5
2024
pubmed:
13
5
2024
entrez:
12
5
2024
Statut:
epublish
Résumé
Biotin, serving as a coenzyme in carboxylation reactions, is a vital nutrient crucial for the natural growth, development, and overall well-being of both humans and animals. Consequently, biotin is widely utilized in various industries, including feed, food, and pharmaceuticals. Despite its potential advantages, the chemical synthesis of biotin for commercial production encounters environmental and safety challenges. The burgeoning field of synthetic biology now allows for the creation of microbial cell factories producing bio-based products, offering a cost-effective alternative to chemical synthesis for biotin production. This review outlines the pathway and regulatory mechanism involved in biotin biosynthesis. Then, the strategies to enhance biotin production through both traditional chemical mutagenesis and advanced metabolic engineering are discussed. Finally, the article explores the limitations and future prospects of microbial biotin production. This comprehensive review not only discusses strategies for biotin enhancement but also provides in-depth insights into systematic metabolic engineering approaches aimed at boosting biotin production.
Identifiants
pubmed: 38735926
doi: 10.1186/s12934-024-02413-1
pii: 10.1186/s12934-024-02413-1
doi:
Substances chimiques
Biotin
6SO6U10H04
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
135Subventions
Organisme : National Natural Science Foundation of China
ID : 22208368
Organisme : National Natural Science Foundation of China
ID : 22178372
Organisme : Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project
ID : TSBICIP-CXRC-070
Organisme : Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project
ID : TSBICIP-KJGG-011
Organisme : National Key R&D Program of China
ID : 2021YFC2100700
Organisme : Youth Innovation Promotion Association, Chinese Academy of Sciences
ID : 2020182
Organisme : Liaoning Province Education Sciences Foundation
ID : LJKMZ20220886
Organisme : National Science Fund for Distinguished Young Scholars
ID : 22325807
Informations de copyright
© 2024. The Author(s).
Références
Lardy HA, Peanasky R. Metabolic functions of biotin. Physiol Rev. 1953;33(4):560–5.
pubmed: 13100070
doi: 10.1152/physrev.1953.33.4.560
McMahon RJ. Biotin in metabolism and molecular biology. Annu Rev Nutr. 2002;22(1):221–39.
pubmed: 12055344
doi: 10.1146/annurev.nutr.22.121101.112819
Said HM. Biotin: biochemical, physiological and clinical aspects. Subcell Biochem. 2012;56:1–19.
pubmed: 22116691
doi: 10.1007/978-94-007-2199-9_1
Wakil SJ, Titchener EB, Gibson DM. Evidence for the participation of biotin in the enzymic synthesis of fatty acids. Biochim Biophys Acta. 1958;29(1):225–6.
pubmed: 13560478
doi: 10.1016/0006-3002(58)90177-X
Wurtele ES, Nikolau BJ. Plants contain multiple biotin enzymes: discovery of 3-methylcrotonyl-CoA carboxylase, propionyl-CoA carboxylase and pyruvate carboxylase in the plant kingdom. Arch Biochem Biophys. 1990;278(1):179–86.
pubmed: 2321957
doi: 10.1016/0003-9861(90)90246-U
Báez-Saldaña A, Zendejas-Ruiz I, Revilla-Monsalve C, Islas-Andrade S, Cárdenas A, Rojas-Ochoa A, Vilches A, Fernandez-Mejia C. Effects of biotin on pyruvate carboxylase, acetyl-CoA carboxylase, propionyl-CoA carboxylase, and markers for glucose and lipid homeostasis in type 2 diabetic patients and nondiabetic subjects. Am J Clin Nutr. 2004;79(2):238–43.
pubmed: 14749229
doi: 10.1093/ajcn/79.2.238
Maurice MS, Reinhardt L, Surinya KH, Attwood PV, Wallace JC, Cleland WW, Rayment I. Domain architecture of pyruvate carboxylase, a biotin-dependent multifunctional enzyme. Science. 2007;317(5841):1076–9.
doi: 10.1126/science.1144504
Hanna M, Jaqua E, Nguyen V, Clay JB. Vitamins: functions and uses in medicine. Perm J. 2002;26:89–97.
doi: 10.7812/TPP/21.204
DeTitta GT, Edmonds JW, Stallings W, Donohue J. Molecular structure of biotin. Results of two independent crystal structure investigations. J Am Chem Soc. 1976;98(7):1920–6.
pubmed: 1254851
doi: 10.1021/ja00423a045
Lane MD, Rominger KL, Young DL, Lynen F. The enzymatic synthesis of holotranscarboxylase from apotranscarboxylase and (+)-biotin: II. Investigation of the reaction mechanism. J Biol Chem. 1964;239(9):2865–71.
pubmed: 14216437
doi: 10.1016/S0021-9258(18)93826-3
Traub W. Crystal structure of biotin. Nature. 1956;178(4534):649–50.
pubmed: 13369496
doi: 10.1038/178649a0
Thompson KG, Kim N. Dietary supplements in dermatology: a review of the evidence for zinc, biotin, vitamin D, nicotinamide, and Polypodium. J Am Acad Dermatol. 2021;84(4):1042–1050.
Nyhan WL. Multiple carboxylase deficiency. Int J Biochem. 1988;20(4):363–70.
pubmed: 3284772
doi: 10.1016/0020-711X(88)90202-9
Seymons K, Moor AD, Raeve HD, Lambert J. Dermatologic signs of biotin deficiency leading to the diagnosis of multiple carboxylase deficiency. Pediatr Dermatol. 2004;21(3):231–5.
pubmed: 15165201
doi: 10.1111/j.0736-8046.2004.21308.x
Báez-Saldana A, Ortega E. Biotin deficiency accelerates thymus involution, blocks thymocyte maturation and decreases noserump length in mice. J Nutr. 2004;134:1979–87.
doi: 10.1093/jn/134.8.1970
Zimmerly CA, Weiss WP. Effects of supplemental dietary biotin on performance of Holstein cows during early lactation. J Dairy Sci. 2001;84:498–506.
pubmed: 11233035
doi: 10.3168/jds.S0022-0302(01)74500-6
Goldberg MW, Montelair U, Sternbach LH. Synthesis of biotin. 1949, United States Patent 2489232A.
Uskokovic MR. Kirk-Othmer Encycl Chem Technology. New York: Wiley; 1984. pp. 41–9.
Xiong F, Chen XX, Chen FE. An improved asymmetric total synthesis of (+)-biotin via the enantioselective desymmetrization of a meso-cyclic anhydride mediated by cinchona alkaloid-based sulfonamide. Tetrahedron-Asymmetr. 2010;21(6):665–9.
doi: 10.1016/j.tetasy.2010.03.041
Streit WR, Entcheva P. Biotin in microbes, the genes involved in its biosynthesis, its biochemical role and perspectives for biotechnological production. Appl Microbiol Biot. 2003;61:21–31.
doi: 10.1007/s00253-002-1186-2
Del Campillo-Campbell A, Kayajanian G, Campbell A, Adhya S. Biotin-requiring mutants of Escherichia coli K-12. J Bacteriol. 1967;94:2065–6.
pubmed: 4864413
pmcid: 276941
doi: 10.1128/jb.94.6.2065-2066.1967
Rolfe B, Eisenberg MA. Genetic and biochemical analysis of the biotin loci of Escherichia coli K-12. J Bacteriol. 1968;96:515–24.
pubmed: 4877129
pmcid: 252325
doi: 10.1128/jb.96.2.515-524.1968
O’Regan M, Gloeckler R, Bernard S, Ledoux C, Ohsawa I, Lemoine Y. Nucleotide sequence of the bioH gene of Escherichia coli. Nucleic Acids Res. 1989;17:8004.
pubmed: 2678009
pmcid: 334922
doi: 10.1093/nar/17.19.8004
Gloeckler R, Ohsawa I, Speck D, Ledoux C, Bernard S, Zinsius M, Villeval D, Kisou T, Kamogawa K. Lemoine Y: Cloning and characterization of the Bacillus sphaericus genes controlling the bioconversion of pimelate into dethiobiotin. Gene. 1990;87:63–70.
pubmed: 2110099
doi: 10.1016/0378-1119(90)90496-E
Bower S, Perkins JB, Yocum RR, Howitt CL, Rahaim P, Pero J. Cloning, sequencing, and characterization of the Bacillus subtilis biotin biosynthetic operon. J Bacteriol. 1996;178:4122–30.
pubmed: 8763940
pmcid: 178169
doi: 10.1128/jb.178.14.4122-4130.1996
Ikeda M, Miyamoto A, Mutoh S, Kitano Y, Tajima M, Shirakura D, Takasaki M, Mitsuhashi S, Takeno S. Development of biotin-prototrophic and -hyperauxotrophic Corynebacterium glutamicum strains. Appl Environ Microbiol. 2013;79:4586–94.
pubmed: 23709504
pmcid: 3719520
doi: 10.1128/AEM.00828-13
Watson RJ, Heys R, Martin T, Savard M. Sinorhizobium meliloti cells require biotin and either cobalt or methionine for growth. Appl Environ Microbiol. 2001;67:3767–70.
pubmed: 11472965
pmcid: 93089
doi: 10.1128/AEM.67.8.3767-3770.2001
Feng Y, Zhang H, Cronan JE. Profligate biotin synthesis in alpha-proteobacteria–a developing or degenerating regulatory system? Mol Microbiol. 2013;88(1):77–92.
pubmed: 23387333
pmcid: 3608792
doi: 10.1111/mmi.12170
Lin S, Cronan JE. The BioC O-methyltransferase catalyzes methyl esterification of malonyl-acyl carrier protein, an essential step in biotin synthesis. J Biol Chem. 2012;287(44):37010–20.
pubmed: 22965231
pmcid: 3481302
doi: 10.1074/jbc.M112.410290
Lin S, Hanson RE, Cronan JE. Biotin synthesis begins by hijacking the fatty acid synthetic pathway. Nat Chem Biol. 2010;6(9):682–8.
pubmed: 20693992
pmcid: 2925990
doi: 10.1038/nchembio.420
Sanishvili R, Yakunin AF, Laskowski RA, Skarina T, Evdokimova E, Doherty-Kirby A, Lajoie GA, Thornton JM, Arrowsmith CH, Savchenko A, Joachimiak A, Edwards AM. Integrating structure, bioinformatics, and enzymology to discover function: BioH, a new carboxylesterase from Escherichia coli. J Biol Chem. 2003;278(28):26039–45.
pubmed: 12732651
doi: 10.1074/jbc.M303867200
Tomczyk NH, Nettleship JE, Baxter RL, Crichton HJ, Webster SP, Campopiano DJ. Purification and characterisation of the BIOH protein from the biotin biosynthetic pathway. Febs Lett. 2002;513(2–3):299–304.
pubmed: 11904168
doi: 10.1016/S0014-5793(02)02342-6
Rodionov DA, Mironov AA, Gelfand MS. Conservation of the biotin regulon and the BirA regulatory signal in Eubacteria and Archaea. Genome Res. 2002;12:1507–16.
pubmed: 12368242
pmcid: 187538
doi: 10.1101/gr.314502
Agarwal V, Lin S, Lukk T, Nair SK, Cronan JE. Structure of the enzyme-acyl carrier protein (ACP) substrate gatekeeper complex required for biotin synthesis. Proc Natl Acad Sci. 2012;109(43):17406–11.
pubmed: 23045647
pmcid: 3491474
doi: 10.1073/pnas.1207028109
Shapiro MM, Chakravartty V, Cronan JE. Remarkable diversity in the enzymes catalyzing the last step in synthesis of the pimelate moiety of biotin. PloS One. 2012;7(11):e49440.
pubmed: 23152908
pmcid: 3494674
doi: 10.1371/journal.pone.0049440
Chow J, Danso D, Ferrer M, Streit WR. The Thaumarchaeon N. gargensis carries functional bioABD genes and has a promiscuous E. Coli ∆bioH-complementing esterase EstN1. Sci Rep. 2018;8(1):13823.
pubmed: 30218044
pmcid: 6138646
doi: 10.1038/s41598-018-32059-0
Bower S, Perkins JB, Yocum RR, Howitt CL, Rahaim P, Pero J. Cloning, sequencing, and characterization of the Bacillus subtilis biotin biosynthetic operon. J Bacteriol. 1996;178(14):4122–30.
pubmed: 8763940
pmcid: 178169
doi: 10.1128/jb.178.14.4122-4130.1996
Stok JE, De Voss JJ. Expression, purification, and characterization of BioI: a carbon–carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis. Arch Biochem Biophys. 2000;384(2):351–60.
pubmed: 11368323
doi: 10.1006/abbi.2000.2067
Cryle MJ, De Voss JJ. Carbon–carbon bond cleavage by cytochrome P450 BioI (CYP107H1). Chem Commun 2004, (1):86–7.
Manandhar M, Cronan JE. A canonical biotin synthesis enzyme, 8-amino-7-oxononanoate synthase (BioF), utilizes different acyl chain donors in Bacillus subtilis and Escherichia coli. Appl Environ Microb. 2018;84(1):e02084–17.
doi: 10.1128/AEM.02084-17
Meunier B, De Visser SP, Shaik S. Mechanism of oxidation reactions catalyzed by cytochrome p450 enzymes. Chem Rev. 2004;104:3947–80.
pubmed: 15352783
doi: 10.1021/cr020443g
Manandhar M, Cronan JE. Pimelic acid, the first precursor of the Bacillus subtilis biotin synthesis pathway, exists as the free acid and is assembled by fatty acid synthesis. Mol Microbiol. 2017;104:595–607.
pubmed: 28196402
pmcid: 5426962
doi: 10.1111/mmi.13648
Estrada P, Manandhar M, Dong SH, Deveryshetty J, Agarwal V, Cronan JE, Nair SK. The pimeloyl-CoA synthetase BioW defines a new fold for adenylate-forming enzymes. Nat Chem Biol. 2017;13(6):668–74.
pubmed: 28414711
pmcid: 7310518
doi: 10.1038/nchembio.2359
Wang M, Moynié L, Harrison PJ, Kelly V, Piper A, Naismith JH, Campopiano DJ. Using the pimeloyl-CoA synthetase adenylation fold to synthesize fatty acid thioesters. Nat Chem Biol. 2017;13(6):660–7.
pubmed: 28414710
doi: 10.1038/nchembio.2361
Hu Y, Cronan JE. α-proteobacteria synthesize biotin precursor pimeloyl-ACP using BioZ 3-ketoacyl-ACP synthase and lysine catabolism. Nat Commun. 2020;11(1):5598.
pubmed: 33154364
pmcid: 7645780
doi: 10.1038/s41467-020-19251-5
Zhang S, Xu Y, Guan H, Cui T, Liao Y, Wei W, Li J, Hassan BH, Zhang H, Jia X, Ouyang S, Feng Y. Biochemical and structural characterization of the BioZ enzyme engaged in bacterial biotin synthesis pathway. Nat Commun. 2021;12(1):2056.
pubmed: 33824341
pmcid: 8024396
doi: 10.1038/s41467-021-22360-4
Sullivan JT, Brown SD, Yocum RR. Ronson1 CW: the bio operon on the acquired symbiosis island of Mesorhizobium sp. strain R7A includes a novel gene involved in pimeloyl-CoA synthesis. Microbiology. 2001;147(5):1315–22.
pubmed: 11320134
doi: 10.1099/00221287-147-5-1315
Hu Z, Cronan JE. The primary step of biotin synthesis in mycobacteria. Proc Natl Acad Sci. 2020;117(38):23794–801.
pubmed: 32900960
pmcid: 7519262
doi: 10.1073/pnas.2010189117
Alexeev D, Alexeeva M, Baxter RL, Campopiano DJ, Webster SP, Sawyer L. The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. J Mol Biol. 1998;284(2):401–19.
pubmed: 9813126
doi: 10.1006/jmbi.1998.2086
Pinon V, Ravanel S, Douce R, Alban C. Biotin synthesis in plants. The first committed step of the pathway is catalyzed by a cytosolic 7-keto-8-aminopelargonic acid synthase. Plant Physiol. 2005;139(4):1666–76.
pubmed: 16299174
pmcid: 1310550
doi: 10.1104/pp.105.070144
Webster SP, Alexeev D, Campopiano DJ, Watt RM, Alexeeva M, Sawyer L, Baxter RL. Mechanism of 8-amino-7-oxononanoate synthase: spectroscopic, kinetic, and crystallographic studies. Biochemistry. 2000;39(3):516–28.
pubmed: 10642176
doi: 10.1021/bi991620j
Fan S, Li DF, Wang DC, Fleming J, Zhang H, Zhou Y, Zhou L, Zhou J, Chen T, Chen G, Zhang XE, Bi L. Structure and function of Mycobacterium smegmatis 7-keto-8-aminopelargonic acid (KAPA) synthase. Int J Biochem Cell Biol. 2015;58:71–80.
pubmed: 25462832
doi: 10.1016/j.biocel.2014.11.006
Fan S, Li D, Fleming J, Hong Y, Chen T, Zhou L, Bi L, Wang D, Zhang X, Chen G. Purification and X-ray crystallographic analysis of 7-keto-8-aminopelargonic acid (KAPA) synthase from Mycobacterium smegmatis. Acta Crystallogr F. 2014;70(10):1372–5.
doi: 10.1107/S2053230X14018317
Kubota T, Izumi Y. Detection and characterization of a thermophilic biotin biosynthetic enzyme, 7-keto-8-aminopelargonic acid synthase, from various thermophiles. Biosci Biotech Bioch. 2012;76(4):685–90.
doi: 10.1271/bbb.110807
Eisenberg MA, Stoner GL. Biosynthesis of 7, 8-diaminopelargonic acid, a biotin intermediate, from 7-keto-8-aminopelargonic acid and S-adenosyl-L-methionine. J Bacteriol. 1971;108(3):1135–40.
pubmed: 4945185
pmcid: 247197
doi: 10.1128/jb.108.3.1135-1140.1971
Izumi Y, Sato K, Tani Y, Ogata K. 7, 8-Diaminopelargonic acid aminotransferase, an enzyme involved in biotin biosynthesis by microorganisms. Agric Biol Chem. 1975;39(1):175–81.
Pai CH. Biosynthesis of biotin: synthesis of 7, 8-diaminopelargonic acid in cell-free extracts of Escherichia coli. J Bacteriol. 1971;105(3):793–800.
pubmed: 4926682
pmcid: 248502
doi: 10.1128/jb.105.3.793-800.1971
Stoner GL, Eisenberg MA. Purification and properties of 7, 8-diaminopelargonic acid aminotransferase. J Biol Chem. 1975;250(11):4029–36.
pubmed: 1092681
doi: 10.1016/S0021-9258(19)41381-1
Mann S, Ploux O. Pyridoxal-5′-phosphate-dependent enzymes involved in biotin biosynthesis: structure, reaction mechanism and inhibition. Biochim Biophys Acta Proteins Proteom. 2011;1814(11):1459–66.
doi: 10.1016/j.bbapap.2010.12.004
Roje S. S-Adenosyl-L-methionine: beyond the universal methyl group donor. Phytochemistry. 2006;67(15):1686–98.
pubmed: 16766004
doi: 10.1016/j.phytochem.2006.04.019
Stoner GL, Eisenberg MA. Biosynthesis of 7, 8-diaminopelargonic acid from 7-keto-8-aminopelargonic acid and S-adenosyl-L-methionine. The kinetics of the reaction. J Biol Chem. 1975;250(11):4037–43.
pubmed: 1092682
doi: 10.1016/S0021-9258(19)41382-3
Wilson DJ, Shi C, Duckworth BP, Muretta JM, Manjunatha U, Sham YY, Thomas DD, Aldrich CC. A continuous fluorescence displacement assay for BioA: an enzyme involved in biotin biosynthesis. Anal Biochem. 2011;416(1):27–38.
pubmed: 21621502
pmcid: 3135573
doi: 10.1016/j.ab.2011.05.003
Van Arsdell SW, Perkins JB, Yocum RR, Luan L, Howitt CL, Prasad Chatterjee N, Pero JG. Removing a bottleneck in the Bacillus subtilis biotin pathway: BioA utilizes lysine rather than S-adenosylmethionine as the amino donor in the KAPA-to-DAPA reaction. Biotechnol Bioeng. 2005;91(1):75–83.
pubmed: 15880481
doi: 10.1002/bit.20488
Salaemae W, Booker GW, Polyak SW. The role of biotin in bacterial physiology and virulence: a novel antibiotic target for Mycobacterium tuberculosis. Microbiol Spectr. 2016;4:797–822.
doi: 10.1128/microbiolspec.VMBF-0008-2015
Casalena D, Nag PP, Park SW, Wilson D, Edwankar R, Johnston S, Le H, Schilling R, Bittker JA, Dandapani S, Munoz B, Dai R, Finzel BC, Schnappinger D, Aldrich C, Schreiber S, Palmer M. Discovery of small molecule probe that shows anti-tubercular activity via Mtb bioA (DAPA synthase) enzyme inhibition. 2015, In: Probe Reports from the NIH Molecular Libraries Program.
Park SW, Casalena DE, Wilson DJ, Dai R, Nag PP, Liu F, Boyce JP, Bittker JA, Schreiber SL, Finzel BC, Schnappinger D, Courtney C, Aldrich CC. Target-based identification of whole-cell active inhibitors of biotin biosynthesis in Mycobacterium tuberculosis. Chem Biol. 2015;22(1):76–86.
pubmed: 25556942
doi: 10.1016/j.chembiol.2014.11.012
Eiden CG, Aldrich CC. Synthesis of a 3-Amino-2, 3-dihydropyrid-4-one and related heterocyclic analogues as mechanism-based inhibitors of BioA, a pyridoxal phosphate-dependent enzyme. J Org Chem. 2017;82(15):7806–19.
pubmed: 28682613
pmcid: 5590672
doi: 10.1021/acs.joc.7b00847
Alexeev D, Baxter RL, Smekal O, Sawyer L. Substrate binding and carboxylation by dethiobiotin synthetase—a kinetic and X-ray study. Structure. 1995;3(11):1207–15.
pubmed: 8591031
doi: 10.1016/S0969-2126(01)00256-8
Sandalova T, Schneider G, Käck H, Lindqvist Y. Structure of dethiobiotin synthetase at 0.97 Å resolution. Acta Crystallogr D. 1999;55(3):610–24.
pubmed: 10089457
doi: 10.1107/S090744499801381X
Huang W, Jia J, Gibson KJ, Taylor WS, Rendina AR, Schneider G, Lindqvist Y. Mechanism of an ATP-dependent carboxylase, dethiobiotin synthetase, based on crystallographic studies of complexes with substrates and a reaction intermediate. Biochemistry. 1995;34(35):10985–95.
pubmed: 7669756
doi: 10.1021/bi00035a004
Salaemae W, Yap MY, Wegener KL, Booker GW, Wilce MC, Polyak SW. Nucleotide triphosphate promiscuity in Mycobacterium tuberculosis dethiobiotin synthetase. Tuberculosis. 2015;95(3):259–66.
pubmed: 25801336
doi: 10.1016/j.tube.2015.02.046
Rendina AR, Taylor WS, Gibson K, Lorimer G, Rayner D, Lockett B, Kranis K, Wexler B, Marcovici-Mizrahi D, Nudelman A, Nudelman A, Marsilii E, Chi H, Wawrzak Z, Calabrese J, Huang W, Jia J, Schneider G, Lindqvist Y, Yang G. The design and synthesis of inhibitors of dethiobiotin synthetase as potential herbicides. Pestic Sci. 1999;55(3):236–47.
doi: 10.1002/(SICI)1096-9063(199903)55:3<236::AID-PS888>3.0.CO;2-0
Schumann NC, Lee KJ, Thompson AP, Salaemae W, Pederick JL, Avery T, Gaiser BI, Hodgkinson-Bean J, Booker GW, Polyak SW, Bruning JB, Wegener KL, Abell AD. Inhibition of Mycobacterium tuberculosis Dethiobiotin synthase (Mt DTBS): toward Next-Generation Antituberculosis agents. Acs Chem Biol. 2021;16(11):2339–47.
pubmed: 34533923
doi: 10.1021/acschembio.1c00491
Fugate CJ, Jarrett JT. Biotin synthase: insights into radical-mediated carbon–sulfur bond formation. Biochim Biophys Acta Proteins Proteom. 2012;1824(11):1213–22.
doi: 10.1016/j.bbapap.2012.01.010
Choi-Rhee E, Cronan JE. A nucleosidase required for in vivo function of the S-adenosyl-L-methionine radical enzyme, biotin synthase. Chem Biol. 2005;12(5):589–93.
pubmed: 15911379
doi: 10.1016/j.chembiol.2005.04.012
Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL. Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme. Science. 2004;303(5654):76–9.
pubmed: 14704425
pmcid: 1456065
doi: 10.1126/science.1088493
Jarrett JT. The novel structure and chemistry of iron–sulfur clusters in the adenosylmethionine-dependent radical enzyme biotin synthase. Arch Biochem Biophys. 2005;433(1):312–21.
pubmed: 15581586
doi: 10.1016/j.abb.2004.10.003
Lotierzo M, Tse Sum Bui B, Florentin D, Escalettes F, Marquet A. Biotin synthase mechanism: an overview. Biochem Soc T. 2005;33(4):820–3.
doi: 10.1042/BST0330820
Yu P, Zhu P. Improving the production of S-adenosyl-L-methionine in Escherichia coli by overexpressing metk. Prep Biochem Biotech. 2017;47(9):867–73.
doi: 10.1080/10826068.2017.1350976
Ollagnier-de-Choudens S, Mulliez E, Fontecave M. The PLP-dependent biotin synthase from Escherichia coli: mechanistic studies. Febs Lett. 2002;532(3):465–8.
pubmed: 12482614
doi: 10.1016/S0014-5793(02)03733-X
Challand MR, Ziegert T, Douglas P, Wood RJ, Kriek M, Shaw NM, Roach PL. Product inhibition in the radical S-adenosylmethionine family. Febs Lett. 2009;583(8):1358–62.
pubmed: 19328201
doi: 10.1016/j.febslet.2009.03.044
Parveen N, Cornell KA. Methylthioadenosine/S-adenosylhomocysteine nucleosidase, a critical enzyme for bacterial metabolism. Mol Microbiol. 2011;79(1):7–20.
pubmed: 21166890
doi: 10.1111/j.1365-2958.2010.07455.x
Baussier C, Fakroun S, Aubert C, Dubrac S, Mandin P, Py B, Barras F. Making iron-sulfur cluster: structure, regulation and evolution of the bacterial ISC system. Adv Microb Physiol. 2020;76:1–39.
pubmed: 32408945
doi: 10.1016/bs.ampbs.2020.01.001
Esquilin-Lebron K, Dubrac S, Barras F, Boyd JM. Bacterial approaches for assembling iron-sulfur proteins. Mbio. 2021;12(6):e0242521.
pubmed: 34781750
doi: 10.1128/mBio.02425-21
Sirithanakorn C, Cronan JE. Biotin, a universal and essential cofactor: synthesis, ligation and regulation. Fems Microbiol Rev. 2021;45(4):fuab003.
pubmed: 33428728
pmcid: 8371270
doi: 10.1093/femsre/fuab003
Cleary PP, Campbell A, Chang R. Location of promoter and operator sites in the biotin gene cluster of Escherichia coli. Proc Natl Acad Sci. 1972;69(8):2219–23.
pubmed: 4559599
pmcid: 426904
doi: 10.1073/pnas.69.8.2219
Hebbeln P, Rodionov DA, Alfandega A, Eitinger T. Biotin uptake in prokaryotes by solute transporters with an optional ATP-binding cassette-containing module. Proc Natl Acad Sci. 2007;104(8):2909–14.
pubmed: 17301237
pmcid: 1815280
doi: 10.1073/pnas.0609905104
Acevedo-Rocha CG, Gronenberg LS, Mack M, Commichau FM, Genee HJ. Microbial cell factories for the sustainable manufacturing of B vitamins. Curr Opin Biotech. 2019;56:18–29.
pubmed: 30138794
doi: 10.1016/j.copbio.2018.07.006
Satiaputra J, Shearwin KE, Booker GW, Polyak SW. Mechanisms of biotin-regulated gene expression in microbes. Syn Syst Biotechnol. 2016;1(1):17–24.
doi: 10.1016/j.synbio.2016.01.005
Rodionov DA, Gelfand MS. Computational identification of BioR, a transcriptional regulator of biotin metabolism in Alphaproteobacteria, and of its binding signal. Fems Microbiol Lett. 2006;255(1):102–7.
pubmed: 16436068
doi: 10.1111/j.1574-6968.2005.00070.x
Tang Q, Li X, Zou T, Zhang H, Wang Y, Gao R, Li Z, He J, Feng Y. Mycobacterium smegmatis BioQ defines a new regulatory network for biotin metabolism. Mol Microbiol. 2014;94(5):1006–23.
doi: 10.1111/mmi.12817
Beckett D. Biotin sensing: universal influence of biotin status on transcription. Annu Rev Genet. 2007;41:443–64.
pubmed: 17669049
doi: 10.1146/annurev.genet.41.042007.170450
Paparella AS, Lee KJ, Hayes AJ, Feng J, Feng Z, Cini D, Deshmukh S, Booker GW, Wilce MCJ, Polyak SW, Abell AD. Halogenation of biotin protein ligase inhibitors improves whole cell activity against Staphylococcus aureus. Acs Infect Dis. 2018;4(2):175–84.
pubmed: 29131575
doi: 10.1021/acsinfecdis.7b00134
Ye H, Cai M, Zhang H, Li Z, Wen R, Feng Y. Functional definition of BirA suggests a biotin utilization pathway in the zoonotic pathogen Streptococcus suis. Sci Rep. 2016;6:26479.
pubmed: 27217336
pmcid: 4877710
doi: 10.1038/srep26479
Satiaputra J, Eijkelkamp BA, McDevitt CA, Shearwin KE, Booker GW, Polyak SW. Biotin-mediated growth and gene expression in Staphylococcus aureus is highly responsive to environmental biotin. Appl Microbiol Biot. 2018;102:3793–803.
doi: 10.1007/s00253-018-8866-z
Feng Y, Chin CY, Chakravartty V, Gao R, Crispell EK, Weiss DS, Cronan JE. The atypical occurrence of two biotin protein ligases in Francisella novicida is due to distinct roles in virulence and biotin metabolism. MBio. 2015;6(3):00591–15.
Feng Y, Xu J, Zhang H, Chen Z, Srinivas S. Brucella BioR regulator defines a complex regulatory mechanism for bacterial biotin metabolism. J Bacteriol. 2013;195(15):3451–67.
pubmed: 23729648
pmcid: 3719536
doi: 10.1128/JB.00378-13
Wei W, Zhang Y, Gao R, Li J, Xu Y, Wang S, Ji Q, Feng Y. Crystal structure and acetylation of BioQ suggests a novel regulatory switch for biotin biosynthesis in Mycobacterium smegmatis. Mol Microbiol. 2018;109(5):642–62.
pubmed: 29995988
doi: 10.1111/mmi.14066
Brune I, Götker S, Schneider J, Rodionov DA, Tauch A. Negative transcriptional control of biotin metabolism genes by the TetR-type regulator BioQ in biotin-auxotrophic Corynebacterium glutamicum ATCC 13032. J Biotechnol. 2012;159(3):225–34.
pubmed: 22178235
doi: 10.1016/j.jbiotec.2011.12.001
Ogata K, Izumi Y, Tani Y. The controlling action of actithiazic acid on the biosynthesis of biotin-vitamers by various microorganisms. Agric Biol Chem. 1973;37(5):1079–85.
doi: 10.1080/00021369.1973.10860806
Izumi Y, Fukuda H, Tani Y, Ogata K. Action of 5-(2-thienyl) valeric acid as a biotin antagonist. Biochim Biophys Acta Gen Subj. 1977;499(2):315–7.
doi: 10.1016/0304-4165(77)90014-9
Izumi Y, Fukuda H, Tani Y, Ogata K. The mode of action of 5-(2-thienyl)-valeric acid on biotin biosynthesis. Agric Biol Chem. 1978;42(3):579–84.
Yamada H, Osakai M, Tani Y, Izumi Y. Biotin overproduction by biotin analog-resistant mutants of Bacillus sphaericus. Agric Biol Chem. 1983;47(5):1011–6.
Sakurai N, Imai Y, Masuda M, Komatsubara S, Tosa T. Construction of a biotin-overproducing strain of Serratia marcescens. Appl Environ Microb. 1993;59(9):2857–63.
doi: 10.1128/aem.59.9.2857-2863.1993
Sakurai N, Imai Y, Masuda M, Komatsubara S, Tosa T. Molecular breeding of a biotin-hyperproducing Serratia marcescens strain. Appl Environ Microb. 1993;59(10):3225–32.
doi: 10.1128/aem.59.10.3225-3232.1993
Sakurai N, Imai Y, Masuda M, Komatsubara S, Tosa T. Improvement of a d-biotin-hyperproducing recombinant strain of. 1994;36(1):63–73.
Masuda M, Takahashi K, Sakurai N, Yanagiya K, Komatsubara S, Tosa T: Further improvement of D-biotin production by a recombinant strain of Serratia marcescens. Process Biochem 1995;30(6):553–562.
Sakurai N, Imai Y, Komatsubara S, Tosa T. Integration of the mutated biotin biosynthetic genes to the chromosome of a d-biotin-producing strain of Serratia marcescens. J Ferment Bioeng. 1994;77(6):610–6.
doi: 10.1016/0922-338X(94)90141-4
Hoshino T, Noro A, Tazoe M. Process for the production of d-biotin. United States Patent. 1997;5:922581.
Ifuku O, Haze SI, Kishimoto J, Koga N, Yanagi M, Fukushima S. Sequencing analysis of mutation points in the biotin operon of biotin-overproducing Escherichia coli mutants. Biosci Biotech Bioch. 1993;57(5):760–5.
doi: 10.1271/bbb.57.760
Kanzaki N, Kawamoto T, Matsui J, Nakahama K, Ifuku O. Microorganism resistant to threonine and production of biotin. United States Patent. 2000;6:020173.
Kanzaki N, Kawamoto T, Matsui J, Nakahama K, Ifuku O. Microorganism resistant to threonine analogue and production of biotin. United States Patent. 2001;6:284500.
Ng CY, Farasat I, Maranas CD, Salis HM. Rational design of a synthetic entner-doudoroff pathway for improved and controllable NADPH regeneration. Metab Eng. 2015;29:86–96.
pubmed: 25769287
doi: 10.1016/j.ymben.2015.03.001
Iwahara S, Takasawa S, Tochikura T, Ogata K. Studies on biosynthesis of biotin by microorganisms. Part IV Conversion of dethiobiotin to biotin by various kinds of microorganisms. Agric Biol Chem. 1966;30(4):385–92.
Clack BA, Youngblood AB. Nucleic acid for biotin production. 2008, United States Patent 7423136B.
Westbrook AW, Ren X, Moo-Young M, Chou CP. Metabolic engineering of Bacillus subtilis for L-valine overproduction. Biotechnol Bioeng. 2018;115(11):2778–92.
pubmed: 29981237
doi: 10.1002/bit.26789
Li Y, Cong H, Liu B, Song J, Sun X, Zhang J, Yang Q. Metabolic engineering of Corynebacterium glutamicum for methionine production by removing feedback inhibition and increasing NADPH level. Anton Leeuw. 2016;109:1185–97.
doi: 10.1007/s10482-016-0719-0
Liu L, Li J, Gai Y, Tian Z, Wang Y, Wang T, Liu P, Yuan Q, Ma H, Lee SY, Zhang D. Protein engineering and iterative multimodule optimization for vitamin B6 production in Escherichia coli. Nat Commun. 2023;14(1):5304.
pubmed: 37652926
pmcid: 10471632
doi: 10.1038/s41467-023-40928-0
Kim DK, Gu B, Kim DG, Oh MK. Quorum sensing-based metabolic engineering of the precursor supply in Streptomyces coelicolor to improve heterologous production of neoaureothin. Biotechnol Bioeng. 2023;120(7):2039–44.
pubmed: 37042226
doi: 10.1002/bit.28400
Ohsawa I, Speck D, Kisou T, Hayakawa K, Zinsius M, Gloeckler R, Lemoine Y, Kamogawa K. Cloning of the biotin synthetase gene from Bacillus sphaericus and expression in Escherichia coli and Bacilli. Gene. 1989;80(1):39–48.
pubmed: 2507401
doi: 10.1016/0378-1119(89)90248-5
Sabatie J, Speck D, Reymund J, Hebert C, Caussin L, Weltin D, Gloeckler R, Regan MO, Bernard S, Ledoux C, Ohsawa I, Kamogawa K, Lemoine Y, Brown SW. Biotin formation by recombinant strains of Escherichia coli: influence of the host physiology. J Biotechnol. 1991;20(1):29–49.
pubmed: 1367314
doi: 10.1016/0168-1656(91)90033-R
Shaw NM, Lehner B, Fuhrmann M, Kulla HG, Brass JM, Birch OM, Tinschert A, Venetz D, Venetz V, Sanchez JC, Tonella L, Hochstrasser DF. Biotin production under limiting growth conditions by Agrobacterium/Rhizobium HK4 transformed with a modified Escherichia coli Bio Operon. J Ind Microbiol Biotechnol. 1999;22:590–9.
pubmed: 10455485
doi: 10.1038/sj.jim.2900669
Bali AP, Lennox-Hvenekilde D, Myling-Petersen N, Buerger J, Salomonsen B, Gronenberg LS, Sommer MOA, Hans J. Genee HJ: improved biotin, thiamine, and lipoic acid biosynthesis by engineering the global regulator IscR. Metab Eng. 2020;60:97–109.
pubmed: 32220614
doi: 10.1016/j.ymben.2020.03.005
Wei PP, Zhu FC, Chen CW, Li GS. Engineering a heterologous synthetic pathway in Escherichia coli for efficient production of biotin. Biotechnol Lett. 2021;43:1221–8.
pubmed: 33666816
doi: 10.1007/s10529-021-03108-y
Galano M, van den Dungen MW, van Rij T, Abbas HE. Safety evaluation of food enzymes produced by a safe strain lineage of Bacillus subtilis. Regul Toxicol Pharm. 2021;126:105030.
doi: 10.1016/j.yrtph.2021.105030
Bower SG, Perkins JB. Yocum RR, JG: biotin biosynthesis in Bacillus subtilis.2000. United States Patent 6,057136.
Wu SC, Wong SL. Engineering of a Bacillus subtilis strain with adjustable levels of intracellular biotin for secretory production of functional streptavidin. Appl Environ Microbiol. 2002;68(3):1102–8.
pubmed: 11872456
pmcid: 123784
doi: 10.1128/AEM.68.3.1102-1108.2002
Zhao J, Zuo S, Huang L, Lian J, Xu Z. CRISPR-Cas12a-based genome editing and transcriptional repression for biotin synthesis in Pseudomonas Mutabilis. J Appl Microbiol. 2023;134(3):lxad049.
pubmed: 36914213
doi: 10.1093/jambio/lxad049
Xiao F, Wang H, Shi Z, Huang Q, Huang L, Lian J, Cai J, Xu Z. Multi-level metabolic engineering of Pseudomonas Mutabilis ATCC31014 for efficient production of biotin. Metab Eng. 2020;61:406–15.
pubmed: 31085296
doi: 10.1016/j.ymben.2019.05.005
Saito I, Honda H, Kawabe T, Mukumoto F, Shimizu M, Kobayashi T. Comparison of biotin production by recombinant Sphingomonas sp. under various agitation conditions. Biochem Eng J. 2000;5(2):129–36.
pubmed: 10817818
doi: 10.1016/S1369-703X(00)00050-4
Hong YR, Chen YL, Farh L, Yang WJ, Liao CH, Shiuan D. Recombinant Candida utilis for the production of biotin. Appl Microbiol Biot. 2006;71:211–21.
doi: 10.1007/s00253-005-0133-4
Sakaki K, Ohishi K, Shimizu T, Kobayashi I, Mori N, Matsuda K, Tomita T, Watanabe H, Tanaka K, Kuzuyama T, Nishiyama M. A suicide enzyme catalyzes multiple reactions for biotin biosynthesis in cyanobacteria. Nat Chem Biol. 2020;16(4):415–22.
pubmed: 32042199
doi: 10.1038/s41589-019-0461-9
Lachowicz JC, Lennox-Hvenekilde D, Myling-Petersen N, Salomonsen B, Verkleij G, Acevedo-Rocha CG, Caddell B, Gronenberg LS, Almo SC, Sommer MOA, Genee HJ, Grove TL. Discovery of a biotin synthase that utilizes an auxiliary 4Fe–5S cluster for sulfur insertion. JACS. 2024;146(3):1860–73.