Biology:Aqualysin 1
From HandWiki
| Aqualysin 1 | |||||||||
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| 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 | ||||||||
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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
- ↑ "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. February 1988. doi:10.1111/j.1432-1033.1988.tb13809.x. PMID 3162211.
- ↑ "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. October 1998. doi:10.1271/bbb.62.2035. PMID 9882104.
- ↑ "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. 1998. doi:10.1271/bbb.62.2161.
External links
- Aqualysin+1 at the US National Library of Medicine Medical Subject Headings (MeSH)
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