EC Number |
BRENDA No. |
Title |
Journal |
Volume |
Pages |
Year |
Organism |
PubMed ID |
---|
3.5.1.82 | 668056 |
A metal ion as a cofactor attenuates substrate inhibition in the enzymatic production of a high concentration of D-glutamate using N-acyl-D-glutamate amidohydrolase |
Biotechnol. Lett. |
27 |
1325-1328 |
2005 |
Achromobacter xylosoxidans |
16215833 |
3.5.1.82 | 31926 |
Chemical modification of histidine residue of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. 5f-1 |
Biosci. Biotechnol. Biochem. |
60 |
650-653 |
1996 |
Pseudomonas sp. |
8829533 |
3.5.1.82 | 31926 |
Chemical modification of histidine residue of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. 5f-1 |
Biosci. Biotechnol. Biochem. |
60 |
650-653 |
1996 |
Pseudomonas sp. 5f-1 |
8829533 |
3.5.1.82 | 31925 |
Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1 |
Biosci. Biotechnol. Biochem. |
59 |
1489-1492 |
1995 |
Pseudomonas sp. |
7549100 |
3.5.1.82 | 31925 |
Metal-characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1 |
Biosci. Biotechnol. Biochem. |
59 |
1489-1492 |
1995 |
Pseudomonas sp. 5f-1 |
7549100 |
3.5.1.82 | 669735 |
Molecular chaperones facilitate the soluble expression of N-acyl-D-amino acid amidohydrolases in Escherichia coli |
J. Ind. Microbiol. Biotechnol. |
31 |
421-426 |
2004 |
Achromobacter xylosoxidans |
15338421 |
3.5.1.82 | 31924 |
Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 |
J. Biochem. |
118 |
204-209 |
1995 |
Achromobacter xylosoxidans |
8537313 |
3.5.1.82 | 31927 |
Purification and characterization of N-acyl-D-glutamate amidohydrolase from Pseudomonas sp. strain 5f-1 |
Appl. Environ. Microbiol. |
57 |
2540-2543 |
1991 |
Pseudomonas sp. |
1768127 |
3.5.1.82 | 31928 |
Purification and characterization of N-acyl-D-glutamate deacylase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6 |
FEBS Lett. |
289 |
44-46 |
1991 |
Pseudomonas sp. |
1894006 |