EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
3.5.1.77 | 756214 |
Identification of D-carbamoylase for biocatalytic cascade synthesis of D-tryptophan featuring high enantioselectivity |
Biores. Technol. |
249 |
720-728 |
2018 |
Arthrobacter crystallopoietes |
29096146 |
3.5.1.77 | 756214 |
Identification of D-carbamoylase for biocatalytic cascade synthesis of D-tryptophan featuring high enantioselectivity |
Biores. Technol. |
249 |
720-728 |
2018 |
Arthrobacter crystallopoietes CGMCC1.1926 |
29096146 |
3.5.1.77 | 757449 |
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 |
J. Mol. Graph. Model. |
86 |
35-42 |
2019 |
Bradyrhizobium japonicum |
30336451 |
3.5.1.77 | 757449 |
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 |
J. Mol. Graph. Model. |
86 |
35-42 |
2019 |
Bradyrhizobium japonicum CPAC 15 |
30336451 |
3.5.1.77 | 757449 |
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 |
J. Mol. Graph. Model. |
86 |
35-42 |
2019 |
Bradyrhizobium japonicum SEMIA 5079 |
30336451 |
3.5.1.77 | 656486 |
Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft |
J. Mol. Biol. |
306 |
251-261 |
2001 |
Agrobacterium tumefaciens |
11237598 |
3.5.1.77 | 657376 |
Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases |
Structure |
8 |
729-738 |
2000 |
Agrobacterium sp. |
10903946 |
3.5.1.77 | 657376 |
Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases |
Structure |
8 |
729-738 |
2000 |
Agrobacterium sp. KNK712 |
10903946 |
3.5.1.77 | 669898 |
D-Amino acid production by E. coli co-expressed three genes encoding hydantoin racemase, D-hydantoinase and N-carbamoyl-D-amino acid amidohydrolase |
J. Mol. Catal. B |
32 |
213-218 |
2005 |
Escherichia coli |
- |
3.5.1.77 | 684966 |
Directed evolution and structural analysis of N-carbamoyl-D-amino acid amidohydrolase provide insights into recombinant protein solubility in Escherichia coli |
Biochem. J. |
402 |
429-437 |
2007 |
Ralstonia pickettii |
17121498 |