Structural basis for differentiation between two classes of thiolase: Degradative vs biosynthetic thiolase.
A-mutant-HAL-CoA, A-mutant-hexanal CoA complex
A-mutant-Hex-CoA, A-mutant-Hexanoyl CoA complex
A-mutants, H356A Mutant
AA-mutants, H356A-C386A Mutant
AS-mutant-OAL-CoA, AS-mutant-octanal CoA complex
AS-mutant-Oct-CoA, AS-mutant-Octanoyl CoA complex
AS-mutants, H356A-C90S Mutant
Covalent locking
Covering loop
HAL, hexanal
Hex-CoA, Hexanoyl CoA
Hexanoyl CoA
Mtb-thiolase, Mycobacterium tuberculosis thiolase
OAL, octanal
Oct-CoA, Octanoyl CoA
Octanoyl CoA
PcaF, β-ketoadipyl-CoA thiolase
Tunnel
Zr-thiolase, Zoogleria ramigera thiolase
Journal
Journal of structural biology: X
ISSN: 2590-1524
Titre abrégé: J Struct Biol X
Pays: United States
ID NLM: 101761384
Informations de publication
Date de publication:
2020
2020
Historique:
received:
27
09
2019
revised:
17
12
2019
accepted:
27
12
2019
entrez:
11
7
2020
pubmed:
11
7
2020
medline:
11
7
2020
Statut:
epublish
Résumé
Thiolases are a well characterized family of enzymes with two distinct categories: degradative, β-ketoadipyl-CoA thiolases and biosynthetic, acetoacetyl-CoA thiolases. Both classes share an identical catalytic triad but catalyze reactions in opposite directions. Moreover, it is established that in contrast to the biosynthetic thiolases the degradative thiolases can accept substrates with broad chain lengths. Hitherto, no residue or structural pattern has been recognized that might help to discern the two thiolases, here we exploit, a tetrameric degradative thiolase from
Identifiants
pubmed: 32647822
doi: 10.1016/j.yjsbx.2019.100018
pii: S2590-1524(19)30016-9
pii: 100018
pmc: PMC7337054
doi:
Types de publication
Journal Article
Langues
eng
Pagination
100018Informations de copyright
© 2020 The Authors.
Déclaration de conflit d'intérêts
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
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