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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 
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 
2021-04-07 | PXD024015 | Pride
Non-ribosomal peptide  biosynthesis  condensation domain  peptidyl carrier protein  biocatalysis 
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 
UnknownDrosophila melanogaster nonribosomal peptide synthetase Ebony encodes an atypical condensation domain.
Not available
S-EPMC6386674 | biostudies-literature
UnknownCrystal structure of the condensation domain from lovastatin polyketide synthase.
Not available
S-EPMC6260248 | biostudies-literature
UnknownThe biosynthetic implications of late-stage condensation domain selectivity during glycopeptide antibiotic biosynthesis.
Not available
S-EPMC6333238 | biostudies-literature
UnknownSubstrate-induced condensation activates plant TIR domain proteins.
Not available
S-EPMC10972746 | biostudies-literature
UnknownStructures of a non-ribosomal peptide synthetase condensation domain suggest the basis of substrate selectivity.
Not available
S-EPMC8097023 | biostudies-literature
UnknownHigh-throughput reprogramming of an NRPS condensation domain.
Not available
S-EPMC11142918 | biostudies-literature
Methylation profilingPerturbation of TET2 condensation induces genome-wide promiscuous DNA hypomethylation and curtails leukemia cell growth
The Ten-Eleven Translocation (TET)-mediated DNA modification pathway is intimately involved in transcriptional regulation. As the major catalytic product of TET enzymes, 5-hydroxymethylcytosine (5hmC) is enriched at selected enhancers in a tissue specific manner, with the underlying mechanism yet to...
ORGANISM(S): Homo sapiens Mus musculus 
2024-06-16 | GSE183934 | GEO
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