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Information on EC 1.21.3.1 - isopenicillin-N synthase and Organism(s) Streptomyces clavuligerus and UniProt Accession P10621

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IUBMB Comments
Forms part of the penicillin biosynthesis pathway (for pathway, click here).
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This record set is specific for:
Streptomyces clavuligerus
UNIPROT: P10621
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Word Map
The taxonomic range for the selected organisms is: Streptomyces clavuligerus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
isopenicillin n synthase, isopenicillin n synthetase, isopenicillin n-synthase, isopenicillin-n synthase, ipn synthase, isopenicillin-n-synthase, isopenicillin n synthase (cyclase), more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isopenicillin-N-synthase
-
isopenicillin N synthase
-
-
-
-
isopenicillin N synthetase
-
-
-
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synthetase, isopenicillin N (9Cl)
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
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oxidative cyclization
-
-
SYSTEMATIC NAME
IUBMB Comments
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine:oxygen oxidoreductase (cyclizing)
Forms part of the penicillin biosynthesis pathway (for pathway, click here).
CAS REGISTRY NUMBER
COMMENTARY hide
78642-31-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
show the reaction diagram
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
show the reaction diagram
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + H2O
show the reaction diagram
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
-
wild-type and mutants, binds to Cys104 in the active site
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ascorbic acid
-
-
dithiothreitol
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000000125
-
mutant C104S, recombinant, partially purified
0.000000177
-
mutant C251S, recombinant, partially purified
0.000000257
-
mutant C142S, recombinant, partially purified
0.000000276
-
mutant C37S, recombinant, partially purified
0.000000338
-
wild-type, recombinant, partially purified
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
IPNS_STRCL
329
0
36959
Swiss-Prot
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C104S
-
single-strand-site-directed mutagenesis, loss of more than 96% activity
C142S
-
single-strand-site-directed mutagenesis, loss of 24% activity
C251S
-
single-strand-site-directed mutagenesis, loss of 47.7% activity
C37S
-
single-strand-site-directed mutagenesis, loss of 18.3% activity
C37S/C142S/C251S
-
triple mutant, conformationally different from wild-type, prepared by recombining fragments of IPNS-encoding gene pcbC from each of the single mutants, loss of more than 90% activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
partially, wild-type and mutants recombinant from Escherichia coli
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutants in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rollins, M.J.; Jensen, S.E.; Westlake, D.W.S.
Isopenicillin N synthase and desacetoxycephalosporin C synthase activities during defined medium fermentations of Streptomyces clavuligerus: effect of oxygen and iron supplements
Can. J. Microbiol.
35
1111-1117
1989
Streptomyces clavuligerus
Manually annotated by BRENDA team
Durairaj, M.; Leskiw, B.K.; Jensen, S.E.
Genetic and biochemical analysis of the cysteinyl residues of isopenicillin N synthase from Streptomyces clavuligerus
Can. J. Microbiol.
42
870-875
1996
Streptomyces clavuligerus
Manually annotated by BRENDA team
Francis, W.R.; Shaner, N.C.; Christianson, L.M.; Powers, M.L.; Haddock, S.H.
Occurrence of isopenicillin-N-synthase homologs in bioluminescent ctenophores and implications for coelenterazine biosynthesis
PLoS ONE
10
e0128742
2015
Acremonium chrysogenum (P05189), Amycolatopsis lactamdurans (P27744), Aspergillus nidulans (P05326), Aspergillus nidulans ATCC 38163 (P05326), Crassostrea gigas (K1QF46), Flavobacterium sp. SC 12154 (P16020), Gordonia rubripertincta, Gordonia rubripertincta NBRC 101908, Lysobacter lactamgenus (Q48739), Mycolicibacterium phlei, Mycolicibacterium phlei RIVM601174, Penicillium chrysogenum (P08703), Streptomyces cattleya (Q53932), Streptomyces clavuligerus (P10621), Streptomyces clavuligerus ATCC 27064 (P10621), Streptomyces griseus (Q54243), Streptomyces jumonjinensis (P18286), Streptomyces microflavus (P12438)
Manually annotated by BRENDA team