Jump to content

Aqualysin 1

From Wikipedia, the free encyclopedia
Aqualysin 1
Identifiers
EC no.3.4.21.111
CAS no.88747-68-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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 ST, Ohta T (February 1988). "Purification and characterization of aqualysin I (a thermophilic alkaline serine protease) produced by Thermus aquaticus YT-1". European Journal of Biochemistry. 171 (3): 441–7. doi:10.1111/j.1432-1033.1988.tb13809.x. PMID 3162211.
  2. ^ Tanaka T, Matsuzawa H, Kojima S, Kumagai I, Miura K, Ohta T (October 1998). "P1 specificity of aqualysin I (a subtilisin-type serine protease) from Thermus aquaticus YT-1, using P1-substituted derivatives of Streptomyces subtilisin inhibitor". Bioscience, Biotechnology, and Biochemistry. 62 (10): 2035–8. doi:10.1271/bbb.62.2035. PMID 9882104.
  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". Bioscience, Biotechnology, and Biochemistry. 62 (11): 2161–5. doi:10.1271/bbb.62.2161.
[edit]