Carboxypeptidase Taq
| Carboxypeptidase Taq | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 3.4.17.19 | ||||||||
| CAS number | 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
- ↑ Lee, S.-H.; Minagawa, E.; Taguchi, H.; Matsuzawa, H.; Ohta, T.; Kaminogawa, S.; Yamauchi, K. (1992). "Purification and characterization of a thermostable carboxypeptidase (carboxypeptidase Taq) from Thermus aquaticus YT-1". Biosci. Biotechnol. Biochem. 56: 1839–1844. doi:10.1271/bbb.56.1839. PMID 1369078.
- ↑ Lee, S.-H.; Taguchi, H.; Yoshimura, E.; Minagawa, E.; Kaminogawa, S.; Ohta, T.; Matsuzawa, H. (1994). "Carboxypeptidase Taq, a thermostable zinc enzyme, from Thermus aquaticus YT-1: molecular cloning, sequencing, and expression of the encoding gene in Escherichia coli". Biosci. Biotechnol. Biochem. 58: 1490–1495. doi:10.1271/bbb.58.1490. PMID 7765282.
External links
- Carboxypeptidase Taq at the US National Library of Medicine Medical Subject Headings (MeSH)
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