Accession | GenProp0909 |
Name | capreomycidine biosynthesis |
Type | PATHWAY |
Description | (2S,3R)-capreomycidine is made as a relatively rare precursor for non-ribosomal peptide synthesis. The first enzyme (VioC), an alpha-ketoglutarate-dependent and Fe(II)-dependent L-arginine beta-hydroxylase, produces (2S,3S)-hydroxyarginine. The second enzyme (VioD), capreomycidine synthase, converts the product to (2S,3R)-capreomycidine. |
JCVI Role | Biosynthesis of natural products |
Parent Property | GenProp0063: biosynthesis
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Literature References | [ 1 ]Helmetag V, Samel SA, Thomas MG, Marahiel MA, Essen LO Structural basis for the erythro-stereospecificity of the L-arginine oxygenase VioC in viomycin biosynthesis. FEBS J. 2009 Jul;276(13):3669-82. Epub 2009 May 26. PMID 19490124 [ 2 ]Ju J, Ozanick SG, Shen B, Thomas MG Conversion of (2S)-arginine to (2S,3R)-capreomycidine by VioC and VioD from the viomycin biosynthetic pathway of Streptomyces sp. strain ATCC11861. Chembiochem. 2004 Sep 6;5(9):1281-5. PMID 15368582 |
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Gene Ontology Term | GO:0042398: cellular modified amino acid biosynthetic process (biological_process)
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