From Wikipedia, the free encyclopedia
Aqualysin 1
Identifiers
EC no. 3.4.21.111
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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

  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.

External links

From Wikipedia, the free encyclopedia
Aqualysin 1
Identifiers
EC no. 3.4.21.111
CAS no. 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
Search
PMC articles
PubMed articles
NCBI proteins

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

  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.

External links


Videos

Youtube | Vimeo | Bing

Websites

Google | Yahoo | Bing

Encyclopedia

Google | Yahoo | Bing

Facebook