KEGG   ENZYME: 1.14.11.40Help
Entry
EC 1.14.11.40               Enzyme                                 

Name
enduracididine beta-hydroxylase;
MppO;
L-enduracididine,2-oxoglutarate:O2 oxidoreductase (3-hydroxylating)
Class
Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
With 2-oxoglutarate as one donor, and incorporation of one atom of oxygen into each donor
BRITE hierarchy
Sysname
L-enduracididine,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Reaction(IUBMB)
L-enduracididine + 2-oxoglutarate + O2 = (3S)-3-hydroxy-L-enduracididine + succinate + CO2 [RN:R10413]
Reaction(KEGG)
Substrate
L-enduracididine [CPD:C20602];
2-oxoglutarate [CPD:C00026];
O2 [CPD:C00007]
Product
(3S)-3-hydroxy-L-enduracididine [CPD:C20603];
succinate [CPD:C00042];
CO2 [CPD:C00011]
Comment
Fe2+-dependent enzyme. The enzyme is involved in biosynthesis of the nonproteinogenic amino acid beta-hydroxyenduracididine, a component of the mannopeptimycins (cyclic glycopeptide antibiotic), produced by Streptomyces hygroscopicus NRRL 30439.
History
EC 1.14.11.40 created 2013
Orthology
K20157  
enduracididine beta-hydroxylase
Reference
1  [PMID:16298295]
  Authors
Haltli B, Tan Y, Magarvey NA, Wagenaar M, Yin X, Greenstein M, Hucul JA, Zabriskie TM
  Title
Investigating beta-hydroxyenduracididine formation in the biosynthesis of the mannopeptimycins.
  Journal
Chem. Biol. 12 (2005) 1163-8.
Reference
2  [PMID:16723579]
  Authors
Magarvey NA, Haltli B, He M, Greenstein M, Hucul JA
  Title
Biosynthetic pathway for mannopeptimycins, lipoglycopeptide antibiotics active against drug-resistant gram-positive pathogens.
  Journal
Antimicrob. Agents. Chemother. 50 (2006) 2167-77.
  Sequence
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 

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