KEGG   ENZYME: 1.21.3.1Help
Entry
EC 1.21.3.1                 Enzyme                                 

Name
isopenicillin-N synthase;
isopenicillin N synthetase
Class
Oxidoreductases;
Acting on X-H and Y-H to form an X-Y bond;
With oxygen as acceptor
BRITE hierarchy
Sysname
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine:oxygen oxidoreductase (cyclizing)
Reaction(IUBMB)
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2 = isopenicillin N + 2 H2O
Reaction(KEGG)
(other) R04872
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Substrate
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine;
O2 [CPD:C00007]
Product
isopenicillin N [CPD:C05557];
H2O [CPD:C00001]
Comment
Forms part of the penicillin biosynthesis pathway (for pathway, click here).
History
EC 1.21.3.1 created 2002
Pathway
Penicillin and cephalosporin biosynthesis
Metabolic pathways
Biosynthesis of secondary metabolites
Orthology
K04126  
isopenicillin-N synthase
Genes
ANI: 
AOR: 
AOR_1_922074(AO090038000544)
AFV: 
PCS: 
ABE: 
TVE: 
SCT: 
SCAT_5683(pcbC)
SCY: 
Taxonomy
Reference
1  [PMID:1588566]
  Authors
Huffman GW, Gesellchen PD, Turner JR, Rothenberger RB, Osborne HE, Miller FD, Chapman JL, Queener SW.
  Title
Substrate specificity of isopenicillin N synthase.
  Journal
J. Med. Chem. 35 (1992) 1897-914.
  Organism
Cephalosporium acremonium, Penicillium chrysogenum
Reference
2  [PMID:7791906]
  Authors
Roach PL, Clifton IJ, Fulop V, Harlos K, Barton GJ, Hajdu J, Andersson I, Schofield CJ, Baldwin JE.
  Title
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes.
  Journal
Nature. 375 (1995) 700-4.
  Organism
Aspergillus nidulans
  Sequence
[ani:AN2622.2]
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
78642-31-6

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