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Literature summary for 3.5.1.49 extracted from

  • 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 (2019), Arch. Biochem. Biophys., 662, 151-159 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
gene amiF, recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 (DE3) Bacillus cereus

Crystallization (Commentary)

Crystallization (Comment) Organism
purified His-tagged enzyme in complex with acetate or urea, mixing of 13 mg/ml protein in 20 mM Tris-HCl, pH 8.0, with PEG448-49, 250 mM urea, pH 4.0, and 20% v/v glycerol in capillaries using the counter-diffusion technique, 20°C, X-ray diffraction structure determination and analysis at 1.78 A and 2.15 A resolution, respectively Bacillus cereus

Inhibitors

Inhibitors Comment Organism Structure
Urea inhibition kinetics and effects on enzyme structure, overview Bacillus cereus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
formamide + H2O Helicobacter pylori
-
formate + NH3
-
?
formamide + H2O Bacillus cereus
-
formate + NH3
-
?
formamide + H2O Bacillus cereus ATCC 14579
-
formate + NH3
-
?
formamide + H2O Bacillus cereus NRRL B-3711
-
formate + NH3
-
?
formamide + H2O Bacillus cereus NCIMB 9373
-
formate + NH3
-
?
formamide + H2O Bacillus cereus CECT 148
-
formate + NH3
-
?
formamide + H2O Bacillus cereus DSM 31
-
formate + NH3
-
?
formamide + H2O Helicobacter pylori ATCC 700392
-
formate + NH3
-
?
formamide + H2O Bacillus cereus NBRC 15305
-
formate + NH3
-
?
formamide + H2O Helicobacter pylori 26695
-
formate + NH3
-
?
formamide + H2O Bacillus cereus JCM 2152
-
formate + NH3
-
?

Organism

Organism UniProt Comment Textmining
Bacillus cereus P59701
-
-
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 26695 O25836
-
-
Helicobacter pylori ATCC 700392 O25836
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and gel filtration Bacillus cereus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
formamide + H2O
-
Helicobacter pylori formate + NH3
-
?
formamide + H2O
-
Bacillus cereus formate + NH3
-
?
formamide + H2O
-
Bacillus cereus ATCC 14579 formate + NH3
-
?
formamide + H2O
-
Bacillus cereus NRRL B-3711 formate + NH3
-
?
formamide + H2O
-
Bacillus cereus NCIMB 9373 formate + NH3
-
?
formamide + H2O
-
Bacillus cereus CECT 148 formate + NH3
-
?
formamide + H2O
-
Bacillus cereus DSM 31 formate + NH3
-
?
formamide + H2O
-
Helicobacter pylori ATCC 700392 formate + NH3
-
?
formamide + H2O
-
Bacillus cereus NBRC 15305 formate + NH3
-
?
formamide + H2O
-
Helicobacter pylori 26695 formate + NH3
-
?
formamide + H2O
-
Bacillus cereus JCM 2152 formate + NH3
-
?

Subunits

Subunits Comment Organism
More enzyme structure analysis by dynamic light scattering, circular dichroism, gel filtration, and mass spectrometry Bacillus cereus

Synonyms

Synonyms Comment Organism
AmiF
-
Helicobacter pylori
AmiF
-
Bacillus cereus
BceAmiF
-
Bacillus cereus
HpyAmiF
-
Helicobacter pylori

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Bacillus cereus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
assay at Bacillus cereus

General Information

General Information Comment Organism
evolution the enzyme is a nitrilase superfamily member Helicobacter pylori
evolution the enzyme is a nitrilase superfamily member Bacillus cereus
additional information a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of Bacillus cereus AmiF and HpyAmiF Helicobacter pylori
additional information a cysteine carbamoyl-switch is responsible for the inhibition of formamidase. Structure comparisons of BceAmiF and Helicobacter pylori AmiF Bacillus cereus