Information on EC 3.5.1.107 - maleamate amidohydrolase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.5.1.107
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RECOMMENDED NAME
GeneOntology No.
maleamate amidohydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
maleamate + H2O = maleate + NH3
show the reaction diagram
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Microbial metabolism in diverse environments
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Nicotinate and nicotinamide metabolism
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nicotinate degradation I
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nicotinate degradation II
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nicotine degradation II (pyrrolidine pathway)
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nicotine degradation III (VPP pathway)
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SYSTEMATIC NAME
IUBMB Comments
maleamate amidohydrolase
The reaction is involved in the aerobic catabolism of nicotinic acid.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain KT2440
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
maleamate + H2O
maleate + NH3
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
maleamate + H2O
maleate + NH3
show the reaction diagram
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aerobic catabolism of nicotinic acid
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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NicF structure and activity do not depend on Zn2+
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.128
Maleamate
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pH 7.5, 25°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
11.7
Maleamate
Bordetella bronchiseptica
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pH 7.5, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44100
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4 * 44100, calculated
86000
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gel fitlration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 2.4 A resolution. Enzyme belongs to the cysteine hydrolase superfamily. The structure shows a conserved catalytic triad, residues Asp29, Lys117, and Cys150, observed in the proximity of a conserved non-proline cis-peptide bond within a small cavity that is likely the active site
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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overexpression in Escherichia coli BL21 (plasmid pETNicF)
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