Biology:Glutamyl endopeptidase II

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Glutamyl endopeptidase II
Identifiers
EC number3.4.21.82
CAS number137010-42-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Glutamyl endopeptidase II (EC 3.4.21.82, GluSGP) is an enzyme.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

Preferential cleavage: -Glu- >> -Asp- . Preference for Pro or Leu at P2 and Phe at P3. Cleavage of -Glu-Asp- and -Glu-Pro- bonds is slow

This enzyme is isolated from Streptomyces griseus.

References

  1. "Purification and characterization of an acidic amino acid specific endopeptidase of Streptomyces griseus obtained from a commercial preparation (Pronase)". Journal of Biochemistry 104 (3): 451–6. September 1988. PMID 3149277. 
  2. "Replacement of P1 Leu18 by Glu18 in the reactive site of turkey ovomucoid third domain converts it into a strong inhibitor of Glu-specific Streptomyces griseus proteinase (GluSGP)". The Journal of Biological Chemistry 266 (17): 10727–30. June 1991. PMID 1674942. 
  3. "Subsite mapping of an acidic amino acid-specific endopeptidase from Streptomyces griseus, GluSGP, and protease V8". Journal of Biochemistry 110 (6): 859–62. December 1991. PMID 1794975. 
  4. "The primary structure of the glutamic acid-specific protease of Streptomyces griseus". FEBS Letters 292 (1-2): 165–7. November 1991. doi:10.1016/0014-5793(91)80859-2. PMID 1959600. 
  5. "Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching". European Journal of Biochemistry 206 (1): 103–7. May 1992. doi:10.1111/j.1432-1033.1992.tb16906.x. PMID 1587264. 

External links