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Information on EC 1.21.3.1 - isopenicillin-N synthase and Organism(s) Streptomyces microflavus and UniProt Accession P12438

for references in articles please use BRENDA:EC1.21.3.1
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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 microflavus
UNIPROT: P12438
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Word Map
The taxonomic range for the selected organisms is: Streptomyces microflavus
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
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isopenicillin N synthase
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-
-
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isopenicillin N synthetase
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-
-
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synthetase, isopenicillin N (9Cl)
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
-
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oxidation
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-
-
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reduction
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-
-
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oxidative cyclization
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-
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
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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 + 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 + H2O
show the reaction diagram
-
-
-
-
?
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine + O2
isopenicillin N + 2 H2O
show the reaction diagram
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common step in the biosynthesis of penicillins, cephalosporins and cephamycins
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Fe2+
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IPNS is a unique mononuclear non-heme Fe enzyme, the enzyme contains [FeNO]7/[FeO2]8 complexes, combination of spectroscopic techniques including EPR, absorbance, circular dichroism, magnetic CD, and variable temperature, variable-field MCD studies of thiolate bonding and the cofactor electronic structure, computational methods and modeling, overview
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.000000093
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purified recombinant enzyme
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_STRMI
333
0
38082
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37800
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x * 37800, DNA sequence determination
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 37800, DNA sequence determination
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant, solubilized enzyme
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli K12 strain JM109 in inclusion bodies
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overexpression in Escherichia coli, DNA sequence analysis
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
dissolution of the recombinant enzyme from Escherichia coli inclusion bodies with 7 M urea containing 20 mM DTT, 30 mM glycine, pH 10.0, requires vigorous stirring for over 2 hours at room temperature
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Loke, P.; Ng, C.P.; Sim, T.S.
PCR cloning, heterologous expression, and characterization of isopenicillin N synthase from Streptomyces lipmanii NRRL 3584
Can. J. Microbiol.
46
166-170
2000
Streptomyces microflavus, Streptomyces microflavus NRRL 3584
Manually annotated by BRENDA team
Brown, C.D.; Neidig, M.L.; Neibergall, M.B.; Lipscomb, J.D.; Solomon, E.I.
VTVH-MCD and DFT studies of thiolate bonding to [FeNO]7/[FeO2]8 complexes of isopenicillin N synthase: substrate determination of oxidase versus oxygenase activity in non-heme Fe enzymes
J. Am. Chem. Soc.
129
7427-7438
2007
Streptomyces microflavus
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