Not always an innocent bystander: the impact of stabilised phosphopantetheine moieties when studying nonribosomal peptide biosynthesis.

Peptide Biosynthesis, Nucleic Acid-Independent Peptide Synthases / chemistry Catalytic Domain Peptides / metabolism Pantetheine

Journal

Chemical communications (Cambridge, England)
ISSN: 1364-548X
Titre abrégé: Chem Commun (Camb)
Pays: England
ID NLM: 9610838

Informations de publication

Date de publication:
29 Jun 2023
Historique:
medline: 3 7 2023
pubmed: 13 6 2023
entrez: 13 6 2023
Statut: epublish

Résumé

Nonribosomal peptide synthetases produce many important peptide natural products and are centred around carrier proteins (CPs) that deliver intermediates to various catalytic domains. We show that the replacement of CP substrate thioesters by stabilised ester analogues leads to active condensation domain complexes, whereas amide stabilisation generates non-functional complexes.

Identifiants

DOI: 10.1039/d3cc01578e PMID: 37310188
pubmed: 37310188
doi: 10.1039/d3cc01578e
doi:

Substances chimiques

4'-phosphopantetheine NM39WU8OFM
Peptide Synthases EC 6.3.2.-
Peptides 0
Pantetheine 496-65-1

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

8234-8237

Auteurs

Y T Candace Ho (YTC)

Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia. max.cryle@monash.edu.
EMBL Australia, Monash University, Clayton, VIC 3800, Australia.
ARC Centre of Excellence for Innovations in Peptide and Protein Science, Australia.
Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK.
ORCID: 0000-0002-8520-9801

Joe A Kaczmarski (JA)

ARC Centre of Excellence in Synthetic Biology, Australian National University, Canberra, Australia.
Research School of Biology, Australian National University, Acton, Australian Capital Territory, Australia.
ORCID: 0000-0001-8549-0122

Julien Tailhades (J)

Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia. max.cryle@monash.edu.
EMBL Australia, Monash University, Clayton, VIC 3800, Australia.
ARC Centre of Excellence for Innovations in Peptide and Protein Science, Australia.
ORCID: 0000-0003-0391-2526

Thierry Izoré (T)

Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia. max.cryle@monash.edu.
EMBL Australia, Monash University, Clayton, VIC 3800, Australia.
ORCID: 0000-0003-0082-0992

David L Steer (DL)

Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia. max.cryle@monash.edu.
Monash Proteomics and Metabolomics Facility, Monash University, Clayton, VIC 3800, Australia.

Ralf B Schittenhelm (RB)

Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia. max.cryle@monash.edu.
Monash Proteomics and Metabolomics Facility, Monash University, Clayton, VIC 3800, Australia.

Manuela Tosin (M)

Department of Chemistry, University of Warwick, Gibbet Hill Road, Coventry, CV4 7AL, UK.
ORCID: 0000-0003-4340-9431

Colin J Jackson (CJ)

ARC Centre of Excellence for Innovations in Peptide and Protein Science, Australia.
ARC Centre of Excellence in Synthetic Biology, Australian National University, Canberra, Australia.
Research School of Biology, Australian National University, Acton, Australian Capital Territory, Australia.
Research School of Chemistry, The Australian National University, Acton, ACT 2601, Australia.

Max J Cryle (MJ)

Department of Biochemistry and Molecular Biology, The Monash Biomedicine Discovery Institute, Monash University, Clayton, VIC 3800, Australia. max.cryle@monash.edu.
EMBL Australia, Monash University, Clayton, VIC 3800, Australia.
ARC Centre of Excellence for Innovations in Peptide and Protein Science, Australia.
ORCID: 0000-0002-9739-6157

Articles similaires

Proteomimetic polymer blocks mitochondrial damage, rescues Huntington's neurons, and slows onset of neuropathology in vivo.

Wonmin Choi, Mara Fattah, Yutong Shang et al.
1.00
Animals Huntington Disease Mitochondria Neurons Mice

PRR adjuvants restrain high stability peptides presentation on APCs.

Bin Li, Jin Zhang, Taojun He et al.
1.00
Animals Adjuvants, Immunologic Mice Antigen-Presenting Cells Antigen Presentation

Encoding extracellular modification of artificial cell membranes using engineered self-translocating proteins.

Alexander Harjung, Alessandro Fracassi, Neal K Devaraj
1.00
Hemolysin Proteins Artificial Cells Protein Engineering Protein Transport Cell Membrane

Catalytic peptide-based coacervates for enhanced function through structural organization and substrate specificity.

David Q P Reis, Sara Pereira, Ana P Ramos et al.
1.00
Substrate Specificity Peptides Catalysis Hydrolysis Protein Conformation

Classifications MeSH

questionsmedicales.fr › Métabolisme › Biosynthèse des peptides › Biosynthèse non ribosomique des peptides › Not always an innocent bystander: the impact...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Ligases › Carbon-nitrogen ligases › Amino-acid ligases › Not always an innocent bystander: the impact...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Éléments structuraux des protéines › Domaine catalytique › Not always an innocent bystander: the impact...
questionsmedicales.fr › Acides aminés, peptides et protéines › Peptides › Not always an innocent bystander: the impact...
questionsmedicales.fr › Composés chimiques organiques › Composés du soufre › Thiols › Pantéthéine › Not always an innocent bystander: the impact...