|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 22.214.171.124
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Mass balance status: Undetermined; a substrate lacks a chemical formula
Enzyme Commission Primary Name: aqualysin 1
Enzyme Commission Synonyms: caldolysin
Enzyme Commission Summary:
This enzyme from the extreme thermophile, Thermus aquaticus, is an alkaline serine peptidase. It has three subsites, S1, S2, and S3, in the substrate binding site. The preferred amino acids at the S1 site are Ala and Phe, at the S2 site are Ala and norleucine and at the S3 site are Phe and Ile. These specificities are similar to those of EC 126.96.36.199 and EC 188.8.131.52. The enzyme displays broad specificity for cleavage of insulin B-chain and hydrolyzes elastin substrates such as succinyl-(Ala)(n)-p nitroanilide (n = 1,2,3) and some peptide esters. Belongs to peptidase family S8A.
The enzyme exhibits low specificity towards esters of amino acids with small hydrophobic or aromatic residues at the P1 position.
Matsuzawa88: Matsuzawa H, Tokugawa K, Hamaoki M, Mizoguchi M, Taguchi H, Terada I, Kwon ST, Ohta T (1988). "Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1." Eur J Biochem 171(3);441-7. PMID: 3162211
Tanaka98a: 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(10);2035-8. PMID: 9882104
©2014 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493