N-carbamoyl-D-amino acid hydrolase
Details
- Name
- N-carbamoyl-D-amino acid hydrolase
- Synonyms
- 3.5.1.77
- D-N-alpha-carbamilase
- Gene Name
- Not Available
- Organism
- Agrobacterium sp. (strain KNK712)
- Amino acid sequence
>lcl|BSEQ0010921|N-carbamoyl-D-amino acid hydrolase MTRQMILAVGQQGPIARAETREQVVVRLLDMLTKAASRGANFIVFPELALTTFFPRWHFT DEAELDSFYETEMPGPVVRPLFEKAAELGIGFNLGYAELVVEGGVKRRFNTSILVDKSGK IVGKYRKIHLPGHKEYEAYRPFQHLEKRYFEPGDLGFPVYDVDAAKMGMFICNDRRWPEA WRVMGLRGAEIICGGYNTPTHNPPVPQHDHLTSFHHLLSMQAGSYQNGAWSAAAGKVGME ENCMLLGHSCIVAPTGEIVALTTTLEDEVITAAVDLDRCRELREHIFNFKQHRQPQHYGL IAEL
- Number of residues
- 304
- Molecular Weight
- 34285.095
- Theoretical pI
- 6.7
- GO Classification
- FunctionsN-carbamoyl-D-amino acid hydrolase activityProcessesnitrogen compound metabolic process
- General Function
- N-carbamoyl-d-amino acid hydrolase activity
- Specific Function
- The enzyme catalyzes the hydrolysis of N-carbamoyl-D-amino acids to the corresponding which are useful intermediates in the preparation of beta-lactam antibiotics. Industrial production of beta-lactam antibiotics is now being developed using this enzyme.
- Pfam Domain Function
- CN_hydrolase (PF00795)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cytoplasmic
- Gene sequence
>lcl|BSEQ0002627|915 bp ATGACACGTCAGATGATACTTGCAGTGGGACAACAAGGTCCGATCGCGCGCGCGGAGACA CGCGAACAGGTCGTCGTTCGTCTTCTCGACATGCTGACGAAAGCCGCGAGCCGGGGCGCG AATTTCATTGTCTTCCCCGAACTCGCGCTTACGACCTTCTTCCCGCGCTGGCATTTCACC GACGAGGCCGAGCTCGATAGCTTCTATGAGACCGAAATGCCCGGCCCGGTGGTCCGTCCA CTCTTTGAGAAGGCCGCGGAACTCGGGATCGGCTTCAATCTGGGCTACGCTGAACTCGTC GTCGAAGGCGGCGTCAAGCGTCGCTTCAACACGTCCATTTTGGTGGATAAGTCAGGCAAG ATCGTCGGCAAGTATCGTAAGATCCATTTGCCGGGTCACAAGGAGTACGAGGCCTACCGG CCGTTCCAGCATCTTGAAAAGCGTTATTTCGAGCCGGGCGATCTCGGCTTCCCGGTCTAT GACGTCGACGCCGCGAAAATGGGGATGTTCATCTGCAACGATCGCCGCTGGCCTGAAGCC TGGCGGGTGATGGGCCTCAGGGGCGCCGAGATCATCTGCGGCGGCTACAACACGCCGACC CACAATCCCCCTGTTCCCCAGCACGACCACCTGACGTCCTTCCACCATCTCCTATCGATG CAGGCCGGGTCTTATCAGAACGGGGCCTGGTCCGCGGCCGCGGGCAAGGTGGGCATGGAG GAGAACTGCATGCTGCTCGGCCACTCCTGCATCGTGGCGCCGACCGGGGAAATCGTCGCT CTCACTACGACGCTGGAAGACGAGGTGATCACCGCCGCCGTCGATCTCGATCGCTGCCGG GAACTGCGTGAACACATCTTCAACTTCAAGCAGCATCGTCAGCCCCAGCACTATGGTCTG ATCGCGGAACTCTGA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P60327 UniProtKB Entry Name DCAS_AGRSK GenBank Protein ID 37896753 GenBank Gene ID AB007368 - General References
- Nanba H, Ikenaka Y, Yamada Y, Yajima K, Takano M, Takahashi S: Isolation of Agrobacterium sp. strain KNK712 that produces N-carbamyl-D-amino acid amidohydrolase, cloning of the gene for this enzyme, and properties of the enzyme. Biosci Biotechnol Biochem. 1998 May;62(5):875-81. [Article]
- Nakai T, Hasegawa T, Yamashita E, Yamamoto M, Kumasaka T, Ueki T, Nanba H, Ikenaka Y, Takahashi S, Sato M, Tsukihara T: Crystal structure of N-carbamyl-D-amino acid amidohydrolase with a novel catalytic framework common to amidohydrolases. Structure. 2000 Jul 15;8(7):729-37. [Article]