1.21.3.1: isopenicillin-N synthase
This is an abbreviated version!
For detailed information about isopenicillin-N synthase, go to the full flat file.
Word Map on EC 1.21.3.1
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1.21.3.1
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chrysogenum
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acremonium
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penicillium
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beta-lactam
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tripeptide
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cephalosporium
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nidulans
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clavuligerus
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delta-l-alpha-aminoadipoyl-l-cysteinyl-d-valine
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deacetoxycephalosporin
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pcbab
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cephamycins
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jumonjinensis
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thiazolidine
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cipns
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lld-acv
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penams
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lactamdurans
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non-haem
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daocs
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biotechnology
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synthesis
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pharmacology
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medicine
- 1.21.3.1
- chrysogenum
- acremonium
- penicillium
- beta-lactam
- tripeptide
- cephalosporium
- nidulans
- clavuligerus
- delta-l-alpha-aminoadipoyl-l-cysteinyl-d-valine
-
deacetoxycephalosporin
-
pcbab
-
cephamycins
- jumonjinensis
- thiazolidine
-
cipns
-
lld-acv
-
penams
- lactamdurans
-
non-haem
- daocs
- biotechnology
- synthesis
- pharmacology
- medicine
Reaction
Synonyms
IPN cyclase, IPN synthase, IPNS, isopenicillin N synthase, isopenicillin N synthase (cyclase), isopenicillin N synthetase, isopenicillin N-synthase, isopenicillin-N synthase, isopenicillin-N-synthase, More, PcbC, synthetase, isopenicillin N (9Cl)
ECTree
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Inhibitors
Inhibitors on EC 1.21.3.1 - isopenicillin-N synthase
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delta-(L-alpha-aminoadipoyl)-L-cysteinyl-D-methionine
substrate analogue, which incorporates a thioether in place of the valinyl sidechain. Crystal structure of the enzyme in complex with the compound and Fe(II) at 1.40 A resolution reveals that the compound binds in the active site such that the sulfur atom of the methionine thioether binds to iron in the oxygen binding site at a distance of 2.57 A. The sulfur of the cysteinyl thiolate sits 2.36 A from the metal
delta-(L-alpha-aminoadipoyl)-L-cysteinyl-O-methyl-D-threonine
substrate analogue, not turned over by IPNS
N-[(5S)-5-amino-5-carboxypentanoyl]-L-cysteinyl-D-valine
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substrate inhibition above 5 mM
NH4+
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inhibition of enzyme formation in vivo, no inhibitory effect in vitro
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only Cys106 can be modified, partly blocked by substrate analogue inhibitors
N-ethylmaleimide
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wild-type and mutants, binds to Cys104 in the active site
additional information
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conversion of the D-valine residue in third position of the enzyme to an aromatic amino acid or to a highly electronegative residue such as trifluorovaline results in elimination of substrate activity and creation of an inhibitor
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additional information
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anions F-, I-, Br-, Cl-, NO3-, H2PO4-, (AsO3)3-, (SO4)2- do not affect the activity; cations Na+, K+, Mg2+, Ca2+, Fe3+ do not affect the activity
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additional information
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ATP, NADPH and FAD: no effect; cations Na+, K+, Mg2+, Ca2+, Fe3+ do not affect the activity
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additional information
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conversion of the D-valine residue in third position of the enzyme to an aromatic amino acid or to a highly electronegative residue such as trifluorovaline results in elimination of substrate activity and creation of an inhibitor
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