Aqualysin 1

Aqualysin 1
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
Search PMC articles PubMed articles NCBI proteins

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

1. Matsuzawa, H., Tokugawa, K., Hamaoki, M., Mizoguchi, M., Taguchi, H., Terada, I., Kwon, S.T. and 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.
2. Tanaka, T., Matsuzawa, H., Kojima, S., Kumagai, I., Miura, K. and 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.
3. Tanaka, T., Matsuzawa, H. and 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)