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UnknownStructural characterization of OxyD, a cytochrome P450 involved in beta-hydroxytyrosine formation in vancomycin biosynthesis.
Not available
S-EPMC2915692 | biostudies-literature
ProteomicsCytochrome P450s protect against oxidative damage via a preferred orientation of the heme cofactor
Cytochrome P450 enzymes (P450s) are a superfamily of monooxygenases that utilise a cysteine thiolate ligated heme moiety to perform a wide range of demanding oxidative transformations. Given the oxidative power of active intermediate formed within P450s during their active cycle, it is remarkable th...
ORGANISM(S): Homo sapiens (Human) 
2022-05-20 | PXD030867 | Pride
Glycopeptide antibiotic (gpa) biosynthesis Cytochrome p450s 
ProteomicsUnderstanding condensation domain selectivity in non-ribosomal peptide biosynthesis: structural characterization of the acceptor bound state
Non-ribosomal peptide synthetases are important enzymes for the assembly of complex peptide natural products. Within these multi-modular assembly lines, condensation domains perform the central function of chain assembly, typically by forming a peptide bond between two peptidyl carrier protein (PCP)...
ORGANISM(S): Escherichia coli 
2021-05-28 | PXD024004 | Pride
Non-ribosomal peptide  biosynthesis  condensation domain  peptidyl carrier protein  biocatalysis 
UnknownF-O-G Ring Formation in Glycopeptide Antibiotic Biosynthesis is Catalysed by OxyE.
Not available
S-EPMC5067714 | biostudies-literature
ProteomicsExploring the selectivity and engineering potential of an NRPS condensation domain involved in the biosynthesis of the thermophilic siderophore fuscachelin
Condensation (C) domains are the key component linking different monomers together, typically forming peptide bonds and occasionally ester bonds, during the nonribosomal peptide synthetase (NRPS). While A domains have been well characterised due to their role in selectivity of the monomers and funct...
ORGANISM(S): Homo sapiens (Human) 
2023-06-02 | PXD040334 | Pride
Nonribosomal peptide  biosynthesis  condensation domain  peptidyl carrier protein  biocatalysis  depsipeptide 
UnknownThe biosynthetic implications of late-stage condensation domain selectivity during glycopeptide antibiotic biosynthesis.
Not available
S-EPMC6333238 | biostudies-literature
UnknownThe archaeal cofactor F0 is a light-harvesting antenna chromophore in eukaryotes.
Not available
S-EPMC2704855 | biostudies-literature
UnknownHalogenation of glycopeptide antibiotics occurs at the amino acid level during non-ribosomal peptide synthesis.
Not available
S-EPMC5620994 | biostudies-literature
UnknownKistamicin biosynthesis reveals the biosynthetic requirements for production of highly crosslinked glycopeptide antibiotics.
Not available
S-EPMC6565677 | biostudies-literature
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