Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.5.1.77 extracted from

  • Bellini, R.G.; Coronado, M.A.; Paschoal, A.R.; Gaudencio do Rego, T.; Hungria, M.; Ribeiro de Vasconcelos, A.T.; Nicolas, M.F.
    Structural analysis of a novel N-carbamoyl-D-amino acid amidohydrolase from a Brazilian Bradyrhizobium japonicum strain in silico insights by molecular modelling, docking and molecular dynamics (2019), J. Mol. Graph. Model., 86, 35-42 .
    View publication on PubMed
Search for more literature for 3.5.1.77

Application

Application Comment Organism
synthesis D-NCAase has wide applications particularly in the pharmaceutical industry, since it catalyzes the production of D-amino acids such as D-p-hydroxyphenylglycine (D-HPG), an intermediate in the synthesis of beta-lactam antibiotics, such as penicillins, cephalosporins and amoxicillin Bradyrhizobium japonicum

Cloned(Commentary)

Cloned (Comment) Organism
gene BJS_06659, sequence comparisons and analysis Bradyrhizobium japonicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
N-carbamoyl-D-4-hydroxyphenylglycine + H2O Bradyrhizobium japonicum
-
 D-4-hydroxyphenylglycine + NH3 + CO2
-
 ?
N-carbamoyl-D-4-hydroxyphenylglycine + H2O Bradyrhizobium japonicum CPAC 15
-
 D-4-hydroxyphenylglycine + NH3 + CO2
-
 ?
N-carbamoyl-D-4-hydroxyphenylglycine + H2O Bradyrhizobium japonicum SEMIA 5079
-
 D-4-hydroxyphenylglycine + NH3 + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Bradyrhizobium japonicum A0A023XI92
-
-
Bradyrhizobium japonicum CPAC 15 A0A023XI92
-
-
Bradyrhizobium japonicum SEMIA 5079 A0A023XI92
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information modeling of the substrate specificity of the catalytic site. The amino acids Lys123, His125, Pro127, Cys172, Asp174 and Arg176 are responsible for recognition of ligand in the active binding site through several chemical associations, such as hydrogen bonds and hydrophobic interactions. Ligand-protein interactions, overview Bradyrhizobium japonicum ?
-
-
additional information modeling of the substrate specificity of the catalytic site. The amino acids Lys123, His125, Pro127, Cys172, Asp174 and Arg176 are responsible for recognition of ligand in the active binding site through several chemical associations, such as hydrogen bonds and hydrophobic interactions. Ligand-protein interactions, overview Bradyrhizobium japonicum CPAC 15 ?
-
-
additional information modeling of the substrate specificity of the catalytic site. The amino acids Lys123, His125, Pro127, Cys172, Asp174 and Arg176 are responsible for recognition of ligand in the active binding site through several chemical associations, such as hydrogen bonds and hydrophobic interactions. Ligand-protein interactions, overview Bradyrhizobium japonicum SEMIA 5079 ?
-
-
N-carbamoyl-D-4-hydroxyphenylglycine + H2O
-
 Bradyrhizobium japonicum D-4-hydroxyphenylglycine + NH3 + CO2
-
 ?
N-carbamoyl-D-4-hydroxyphenylglycine + H2O
-
 Bradyrhizobium japonicum CPAC 15 D-4-hydroxyphenylglycine + NH3 + CO2
-
 ?
N-carbamoyl-D-4-hydroxyphenylglycine + H2O
-
 Bradyrhizobium japonicum SEMIA 5079 D-4-hydroxyphenylglycine + NH3 + CO2
-
 ?

Subunits

Subunits Comment Organism
homodimer structural analysis and molecular dynamics simulations Bradyrhizobium japonicum
homotetramer structure modelling Bradyrhizobium japonicum
More a homotetrameric structure is obtained by homology modelling using structure of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter CCRC 14924 (PDB ID 1FO6), composed of chains A, B, C, and D, but structural analysis and the molecular dynamics simulations suggest that D-NCAase of Bradyrhizobium japonicum strain CPAC-15 has a homodimeric structure in solution. Intersubunit interactions and enzyme structure analysis, molecular modelling, docking and molecular dynamics, overview Bradyrhizobium japonicum

Synonyms

Synonyms Comment Organism
BJS_06659
-
 Bradyrhizobium japonicum
D-NCAase
-
 Bradyrhizobium japonicum
N-carbamoyl-D-amino acid amidohydrolase
-
 Bradyrhizobium japonicum

General Information

General Information Comment Organism
evolution the enzyme belongs to the amidohydrolase superfamily Bradyrhizobium japonicum
additional information intersubunit interactions and enzyme structure analysis, molecular modelling, docking and molecular dynamics, overview Bradyrhizobium japonicum