Information on EC 3.5.1.106 - N-formylmaleamate deformylase

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The expected taxonomic range for this enzyme is: Pseudomonas putida

EC NUMBER
COMMENTARY hide
3.5.1.106
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RECOMMENDED NAME
GeneOntology No.
N-formylmaleamate deformylase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
N-formylmaleamic acid + H2O = maleamate + formate
show the reaction diagram
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-
-
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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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nicotine degradation II (pyrrolidine pathway)
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nicotine degradation III (VPP pathway)
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SYSTEMATIC NAME
IUBMB Comments
N-formylmaleamic acid 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
N-formylmaleamic acid + H2O
maleamate + formate
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
N-formylmaleamic acid + H2O
maleamate + formate
show the reaction diagram
-
aerobic catabolism of nicotinic acid
-
-
?
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
-
x * 29000, SDS-PAGE
29100
-
x * 29100, calculated from sequence
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
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x * 29000, SDS-PAGE; x * 29100, calculated from sequence
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D125A
-
mutation leads to a complete loss of the deformylase activity
E221A
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70% of wild-type deformylase acticity
H245A
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mutation leads to a complete loss of the deformylase activity
S101A
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mutation leads to a complete loss of the deformylase activity