Aqualysin 1

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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

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[edit]

  1. ^ 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. PMID 3162211. doi:10.1111/j.1432-1033.1988.tb13809.x. 
  2. ^ 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. PMID 9882104. doi:10.1271/bbb.62.2035. 
  3. ^ 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[edit]