Aqualysin 1
Aqualysin 1 | |||||||||
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Identifiers | |||||||||
EC number | 3.4.21.111 | ||||||||
CAS number | 88747-68-6 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
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Aqualysin 1 (EC 3.4.21.111, caldolysin) is an enzyme.[1][2][3] This enzyme catalyses the following chemical reaction
- Exhibits low specificity towards esters of amino acids with small hydrophobic or aromatic residues at the P1 position
This enzyme is isolated from the thermophile, Thermus aquaticus.
References
- ↑ Matsuzawa, H.; Tokugawa, K.; Hamaoki, M.; Mizoguchi, M.; Taguchi, H.; Terada, I.; Kwon, S.T.; Ohta, T. (1988). "Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1". Eur. J. Biochem. 171: 441–447. doi:10.1111/j.1432-1033.1988.tb13809.x. PMID 3162211.
- ↑ Tanaka, T.; Matsuzawa, H.; Kojima, S.; Kumagai, I.; Miura, K.; Ohta, T. (1998). "P1 specificity of aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor". Biosci. Biotechnol. Biochem. 62: 2035–2038. doi:10.1271/bbb.62.2035. PMID 9882104.
- ↑ Tanaka, T.; Matsuzawa, H.; Ohta, T. (1998). "Substrate specificity of aqualysin I, a bacterial thermophilic alkaline serine protease from Thermus aquaticus YT-1: Comparison with proteinase K, subtilisin BPN′ and subtilisin Carlsberg". Biosci. Biotechnol. Biochem. 62: 2161–2165. doi:10.1271/bbb.62.2161.
External links
- Aqualysin 1 at the US National Library of Medicine Medical Subject Headings (MeSH)
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