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Information on EC 3.5.1.49 - formamidase and Organism(s) Helicobacter pylori and UniProt Accession O25836
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3.5.1.49 formamidaseIUBMB Comments
Also acts, more slowly, on acetamide, propanamide and butanamide.
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Word Map
- 3.5.1.49
- kynurenine
- urease
-
2,3-dioxygenase
- n-formyl-l-kynurenine
- 2-aminofluorene
- methylotrophus
- methylophilus
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n-formylation
The taxonomic range for the selected organisms is: Helicobacter pylori
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
formamidase, acetamidase/formamidase, bceamif, amds/fmds, amif formamidase, formamide amidohydrolase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Formamide amidohydrolase
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-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxylic acid amide hydrolysis
carboxylic acid amide hydrolysis
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-
-
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PATHWAY SOURCE
PATHWAYS
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-
SYSTEMATIC NAME
IUBMB Comments
formamide amidohydrolase
Also acts, more slowly, on acetamide, propanamide and butanamide.
CAS REGISTRY NUMBER
COMMENTARY
9013-59-6
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
3D structure study is built by homology modeling and catalytic mechanism study
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-
?
formamide + H2O
formate + NH3
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from AmiF gene, that exclusively hydrolyzes formamide, involved in nitrogen metabolism
-
?
formamide + H2O
formate + NH3
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from AmiE gene, very low activity
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.05
0.1
0.5
-
amidase activity wild-type Helicobacter pylori 26695, pH 7.0, 500 micromol NiCl2 supplementation
0.55
-
amidase activity wild-type Helicobacter pylori 26695, pH 7.0, 1000 micromol NiCl2 supplementation
30
-
urease activity wild-type Helicobacter pylori 26695, pH 7.0, 1 micromol NiCl2 supplementation
5.2
-
formamidase activity wild-type Helicobacter pylori 26695, pH 7.0, 1000 micromol NiCl2 supplementation
60
-
urease activity wild-type Helicobacter pylori 26695, pH 7.0, 100 micromol NiCl2 supplementation
70
-
urease activity wild-type Helicobacter pylori 26695, pH 7.0, 1000 micromol NiCl2 supplementation
75
-
urease activity wild-type Helicobacter pylori 26695, pH 7.0, 500 micromol NiCl2 supplementation
8.1
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formamidase activity wild-type Helicobacter pylori 26695, pH 7.0, 100 micromol NiCl2 supplementation
0.05
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amidase activity wild-type Helicobacter pylori 26695, pH 7.0, 0 micromol NiCl2 supplementation
0.05
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amidase activity wild-type Helicobacter pylori 26695, pH 7.0, 1 micromol NiCl2 supplementation
0.1
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amidase activity wild-type Helicobacter pylori 26695, pH 7.0, 100 micromol NiCl2 supplementation
6
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formamidase activity wild-type Helicobacter pylori 26695, pH 7.0, 0 micromol NiCl2 supplementation
6
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formamidase activity wild-type Helicobacter pylori 26695, pH 7.0, 1 micromol NiCl2 supplementation
8
-
formamidase activity wild-type Helicobacter pylori 26695, pH 7.0, 500 micromol NiCl2 supplementation
8
-
urease activity wild-type Helicobacter pylori 26695, pH 7.0, 0 micromol NiCl2 supplementation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of Bacillus cereus AmiF and HpyAmiF
additional information
-
a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of Bacillus cereus AmiF and HpyAmiF
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of AmiF is solved to 1.75 A resolution using single-wavelength anomalous dispersion methods. The structure consists of a homohexamer related by 3fold symmetry in which each subunit has an alpha-beta-beta-alpha four-layer architecture characteristic of the nitrilase superfamily
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
fur mutant
nikR fur double mutant
nikR mutant
fur mutant
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amidase activity at pH 5.5: wild-type 0.6, mutant 3.0 - at pH 7.0: wild-type 0.1, mutant 2.9
fur mutant
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formamidase activity at pH 5.5: wild-type 25, mutant 41 - at pH 7.0: wild-type 5, mutant 41
fur mutant
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urease activity at pH 5.5: wild-type 20, mutant 23 - at pH 7.0: wild-type 4, mutant 3
nikR fur double mutant
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amidase activity at pH 5.5: wild-type 0.6, mutant 1.9 - at pH 7.0: wild-type 0.1, mutant 3.0
nikR fur double mutant
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formamidase activity at pH 5.5: wild-type 25, mutant 30 - at pH 7.0: wild-type 5, mutant 40
nikR fur double mutant
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urease activity at pH 5.5: wild-type 20, mutant 14 - at pH 7.0: wild-type 4, mutant 6
nikR mutant
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amidase activity at pH 5.5: wild-type 0.6, mutant 0.2 - at pH 7.0: wild-type 0.1, mutant 0.1
nikR mutant
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formamidase activity at pH 5.5: wild-type 25, mutant 8 - at pH 7.0: wild-type 5, mutant 5
nikR mutant
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urease activity at pH 5.5: wild-type 20, mutant 13 - at pH 7.0: wild-type 4, mutant 5
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Skouloubris, S.; Labigne, A.; de Reuse H.
Identification and characterization of an aliphatic amidase in Helicobacter pylori
Mol. Microbiol.
25
989-998
1997
Helicobacter pylori
Skouloubris, S.; Labigne, A.; de Reuse H.
The AmiE aliphatic amidase and AmiF formamidase of Helicobacter pylori: natural evolution of two enzyme paralogues
Mol. Microbiol.
40
596-609
2001
Helicobacter pylori
van Vliet, A.H.; Kuipers, E.J.; Stoof, J.; Poppelaars, S.W.; Kusters, J.G.
Acid-responsive gene induction of ammonia-producing enzymes in Helicobacter pylori is mediated via a metal-responsive repressor cascade
Infect. Immun.
72
766-773
2004
Helicobacter pylori
Hung, C.L.; Liu, J.H.; Chiu, W.C.; Huang, S.W.; Hwang, J.K.; Wang, W.C.
Crystal structure of Helicobacter pylori formamidase AmiF reveals a cysteine-glutamate-lysine catalytic triad
J. Biol. Chem.
282
12220-12229
2007
Helicobacter pylori
Han, W.; Zhou, Y.; Luo, Q.; Yao, Y.; Li, Z.
On the 3D structure and catalytic mechanism study of AmiF formamidase of Helicobacter pylori
Polymer
48
3726-3731
2007
Helicobacter pylori (O25836)
-
Martinez-Rodriguez, S.; Conejero-Muriel, M.; Gavira, J.A.
A novel cysteine carbamoyl-switch is responsible for the inhibition of formamidase, a nitrilase superfamily member
Arch. Biochem. Biophys.
662
151-159
2019
Bacillus cereus (P59701), Bacillus cereus, Bacillus cereus ATCC 14579 (P59701), Bacillus cereus CECT 148 (P59701), Bacillus cereus DSM 31 (P59701), Bacillus cereus JCM 2152 (P59701), Bacillus cereus NBRC 15305 (P59701), Bacillus cereus NCIMB 9373 (P59701), Bacillus cereus NRRL B-3711 (P59701), Helicobacter pylori (O25836), Helicobacter pylori, Helicobacter pylori 26695 (O25836), Helicobacter pylori ATCC 700392 (O25836)
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