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Literature summary for 3.5.2.2 extracted from

  • Kao, C.H.; Lo, H.H.; Hsu, S.K.; Hsu, W.H.
    A novel hydantoinase process using recombinant Escherichia coli cells with dihydropyrimidinase and L-N-carbamoylase activities as biocatalyst for the production of L-homophenylalanine (2008), J. Biotechnol., 134, 231-239.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli strain JM109, the expression level of dihydropyrimidinase in the recombinant Escherichia coli cells is estimated to be about 20% of the respective total soluble proteins Brevibacillus agri

Inhibitors

Inhibitors Comment Organism Structure
Zn2+ a loss of 50% activity is observed in the presence of Zn2+ Brevibacillus agri

Metals/Ions

Metals/Ions Comment Organism Structure
Mn2+ the hydrolytic activity of PydB is enhanced notably by 0.5 mM Mn2+, about an 8fold increase in the enzymatic activity is observed in the presence of 0.05-5 mM Mn2+ Brevibacillus agri
additional information other divalent metal ions except Mn2+ and Zn2+ do not have significant effect on the enzyme activity Brevibacillus agri

Organism

Organism UniProt Comment Textmining
Brevibacillus agri
-
-
-
Brevibacillus agri NCHU1002
-
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Brevibacillus agri

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DL-5-(2-methylthioethyl)-hydantoin + H2O the enzyme exhibits strict D-enantioselectivity for DL-5-(2-methylthioethyl)-hydantoin Brevibacillus agri N-carbamoyl-D-methionine
-
?
DL-5-(2-methylthioethyl)-hydantoin + H2O the enzyme exhibits strict D-enantioselectivity for DL-5-(2-methylthioethyl)-hydantoin Brevibacillus agri NCHU1002 N-carbamoyl-D-methionine
-
?
DL-homophenylalanylhydantoin + H2O the enzyme exhibits non-enantiospecificity for DL-homophenylalanylhydantoin Brevibacillus agri ?
-
?
DL-homophenylalanylhydantoin + H2O the enzyme exhibits non-enantiospecificity for DL-homophenylalanylhydantoin Brevibacillus agri NCHU1002 ?
-
?
DL-p-hydroxyphenylhydantoin + H2O the enzyme exhibits strict D-enantioselectivity for DL-p-hydroxyphenylhydantoin Brevibacillus agri N-carbamoyl-D-hydroxyphenylglycine
-
?
DL-p-hydroxyphenylhydantoin + H2O the enzyme exhibits strict D-enantioselectivity for DL-p-hydroxyphenylhydantoin Brevibacillus agri NCHU1002 N-carbamoyl-D-hydroxyphenylglycine
-
?

Synonyms

Synonyms Comment Organism
PydB
-
Brevibacillus agri

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
60
-
-
Brevibacillus agri

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50 90 the enzyme is completely thermostable at 50°C for 20 days, and 50% of its initial activity remains after 36 days of incubation. After that, enzymatic activity gradually decreases to 4.4% after 65 days. Less than 15% maximum activity is observed at 90°C for 10 min. Brevibacillus agri

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
in 50mM Tris-HCl buffer Brevibacillus agri

pH Range

pH Minimum pH Maximum Comment Organism
6 9.5 in 50mM Tris-HCl buffer Brevibacillus agri

pH Stability

pH Stability pH Stability Maximum Comment Organism
5.5
-
the enzyme activity is completely lost below pH 5.5 Brevibacillus agri