From Wikipedia, the free encyclopedia
Mycolysin
Identifiers
EC no. 3.4.24.31
CAS no. 153190-34-2
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

Mycolysin ( EC 3.4.24.31, pronase component, Streptomyces griseus neutral proteinase, actinase E, SGNPI) is an enzyme. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

Preferential cleavage of bonds with hydrophobic residues in P1'

This enzyme is present in Streptomyces griseus, S. naraensis, and S. cacaoi.

References

  1. ^ Morihara K, Tsuzuki H, Oka T (March 1968). "Comparison of the specificities of various neutral proteinases from microorganisms". Archives of Biochemistry and Biophysics. 123 (3): 572–88. doi: 10.1016/0003-9861(68)90179-3. PMID  4967801.
  2. ^ Hiramatsu A, Ouchi T (May 1972). "A neutral proteinase from Streptomyces naraensis. 3. An improved purification and some physiochemical properties". Journal of Biochemistry. 71 (5): 767–81. PMID  5073323.
  3. ^ Blumberg S, Tauber Z (October 1983). "Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides". European Journal of Biochemistry. 136 (1): 151–4. doi: 10.1111/j.1432-1033.1983.tb07719.x. PMID  6413206.
  4. ^ Chang PC, Kuo TC, Tsugita A, Lee YH (March 1990). "Extracellular metalloprotease gene of Streptomyces cacaoi: structure, nucleotide sequence and characterization of the cloned gene product". Gene. 88 (1): 87–95. doi: 10.1016/0378-1119(90)90063-w. PMID  2341042.
From Wikipedia, the free encyclopedia
Mycolysin
Identifiers
EC no. 3.4.24.31
CAS no. 153190-34-2
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

Mycolysin ( EC 3.4.24.31, pronase component, Streptomyces griseus neutral proteinase, actinase E, SGNPI) is an enzyme. [1] [2] [3] [4] This enzyme catalyses the following chemical reaction

Preferential cleavage of bonds with hydrophobic residues in P1'

This enzyme is present in Streptomyces griseus, S. naraensis, and S. cacaoi.

References

  1. ^ Morihara K, Tsuzuki H, Oka T (March 1968). "Comparison of the specificities of various neutral proteinases from microorganisms". Archives of Biochemistry and Biophysics. 123 (3): 572–88. doi: 10.1016/0003-9861(68)90179-3. PMID  4967801.
  2. ^ Hiramatsu A, Ouchi T (May 1972). "A neutral proteinase from Streptomyces naraensis. 3. An improved purification and some physiochemical properties". Journal of Biochemistry. 71 (5): 767–81. PMID  5073323.
  3. ^ Blumberg S, Tauber Z (October 1983). "Inhibition of metalloendopeptidases by 2-mercaptoacetyl-dipeptides". European Journal of Biochemistry. 136 (1): 151–4. doi: 10.1111/j.1432-1033.1983.tb07719.x. PMID  6413206.
  4. ^ Chang PC, Kuo TC, Tsugita A, Lee YH (March 1990). "Extracellular metalloprotease gene of Streptomyces cacaoi: structure, nucleotide sequence and characterization of the cloned gene product". Gene. 88 (1): 87–95. doi: 10.1016/0378-1119(90)90063-w. PMID  2341042.

Videos

Youtube | Vimeo | Bing

Websites

Google | Yahoo | Bing

Encyclopedia

Google | Yahoo | Bing

Facebook