Carboxypeptidase Taq
| Carboxypeptidase Taq | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.19 | ||||||||
| CAS no. | 9031-98-5 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Carboxypeptidase Taq (EC 3.4.17.19) is an enzyme.[1][2] This enzyme catalyses the following chemical reaction
- Release of a C-terminal amino acid with broad specificity, except for -Pro
This 56-kDa enzyme is isolated from Thermus aquaticus.
References
[edit]- ^ Lee SH, Minagawa E, Taguchi H, Matsuzawa H, Ohta T, Kaminogawa S, Yamauchi K (November 1992). "Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1". Bioscience, Biotechnology, and Biochemistry. 56 (11): 1839–44. doi:10.1271/bbb.56.1839. PMID 1369078.
- ^ Lee SH, Taguchi H, Yoshimura E, Minagawa E, Kaminogawa S, Ohta T, Matsuzawa H (August 1994). "Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli". Bioscience, Biotechnology, and Biochemistry. 58 (8): 1490–5. doi:10.1271/bbb.58.1490. PMID 7765282.
External links
[edit]- Carboxypeptidase+Taq at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
