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Literature summary for 4.2.1.49 extracted from

  • Kaminskas, E.; Kimhi, Y.; Magasanik, B.
    Urocanase and N-formimino-L-glutamate formiminohydrolase of Bacillus subtilis, two enzymes of the histidine degradation pathway (1970), J. Biol. Chem., 245, 3536-3544.
    View publication on PubMed
Search for more literature for 4.2.1.49

General Stability

General Stability Organism
highly unstable enzyme, pyridoxal 5'-phosphate partially stabilizes Bacillus subtilis

Inhibitors

Inhibitors Comment Organism Structure
Imidazolepropionate competitive Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.077
-
 Urocanate
-
 Bacillus subtilis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
 2 * 60000, SDS-PAGE Bacillus subtilis
120000
-
 sucrose density gradient centrifugation Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
Urocanate + H2O Salmonella enterica subsp. enterica serovar Typhimurium
-
 ?
-
 ?
Urocanate + H2O Klebsiella aerogenes
-
 ?
-
 ?
Urocanate + H2O Bacillus subtilis an enzyme in the histidine catabolism ?
-
 ?
Urocanate + H2O Bacillus subtilis SH-11 an enzyme in the histidine catabolism ?
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
 derived from SB 19
-
Bacillus subtilis SH-11
-
 derived from SB 19
-
Klebsiella aerogenes
-
-
-
Salmonella enterica subsp. enterica serovar Typhimurium
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Bacillus subtilis

Reaction

Reaction Comment Organism Reaction ID
3-(5-oxo-4,5-dihydro-3H-imidazol-4-yl)propanoate = urocanate + H2O enzyme catalyzes a complex reaction involving an intramolecular oxidation-reduction with the addition of a molecule of water and a conversion of the imidazole ring into a highly unstable imidazolone ring Bacillus subtilis
a

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.278
-
-
 Bacillus subtilis

Storage Stability

Storage Stability Organism
-20¦C, 40% loss of activity after 3 months Bacillus subtilis
addition of glycerol to a final concentration of 50% prevents inactivation of the enzyme at 4¦C Bacillus subtilis
presence of 0.01 M 2-mercaptoethanol in the buffer results in total inactivation of the enzyme upon freezing Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Urocanate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium 4,5-Dihydro-4-oxo-5-imidazolepropanoate
-
 ?
Urocanate + H2O
-
 Bacillus subtilis 4,5-Dihydro-4-oxo-5-imidazolepropanoate
-
 ?
Urocanate + H2O
-
 Klebsiella aerogenes 4,5-Dihydro-4-oxo-5-imidazolepropanoate
-
 ?
Urocanate + H2O
-
 Bacillus subtilis SH-11 4,5-Dihydro-4-oxo-5-imidazolepropanoate
-
 ?
Urocanate + H2O
-
 Salmonella enterica subsp. enterica serovar Typhimurium ?
-
 ?
Urocanate + H2O
-
 Klebsiella aerogenes ?
-
 ?
Urocanate + H2O an enzyme in the histidine catabolism Bacillus subtilis ?
-
 ?
Urocanate + H2O an enzyme in the histidine catabolism Bacillus subtilis SH-11 ?
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 60000, SDS-PAGE Bacillus subtilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 5 min, 60% loss of activity Bacillus subtilis
60
-
 5 min, 80% loss of activity Bacillus subtilis
70
-
 5 min, 100% loss of activity Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.2 8
-
 Bacillus subtilis