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Results 1 - 10 of 48 > >>
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EC Number BRENDA No. Title Journal Volume Pages Year Organism PubMed ID
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.77756214 Identification of D-carbamoylase for biocatalytic cascade synthesis of D-tryptophan featuring high enantioselectivity Biores. Technol. 249 720-728 2018 Arthrobacter crystallopoietes 29096146
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.77756214 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
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.77757449 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
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.77757449 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
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.77757449 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
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.77656486 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
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.77657376 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
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.77657376 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
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.77669898 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 -
Display the word mapDisplay the reaction diagram Show all sequences 3.5.1.77684966 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
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