MetaCyc Reaction:

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number:

Enzymes and Genes:

Thermus aquaticus YT-1 : aqualysin I Inferred from experiment : pstI

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction in which it was curated.

Mass balance status: Balance undetermined; a substrate lacks a chemical formula

Enzyme Commission Primary Name: aqualysin 1

Enzyme Commission Synonyms: caldolysin

Taxonomic Range: Bacteria

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 and EC 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.

Citations: [Tanaka98, Matsuzawa88]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Relationship Links: BRENDA:EC: , ENZYME:EC: , IUBMB-ExplorEnz:EC:


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

Tanaka98: 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

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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
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