Glutamyl endopeptidase II

Glutamyl endopeptidase II
Identifiers
EC no.3.4.21.82
CAS no.137010-42-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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NCBIproteins

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.

  1. ^ Yoshida N, Tsuruyama S, Nagata K, Hirayama K, Noda K, Makisumi S (September 1988). "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. PMID 3149277.
  2. ^ Komiyama T, Bigler TL, Yoshida N, Noda K, Laskowski M (June 1991). "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. PMID 1674942.
  3. ^ Nagata K, Yoshida N, Ogata F, Araki M, Noda K (December 1991). "Subsite mapping of an acidic amino acid-specific endopeptidase from Streptomyces griseus, GluSGP, and protease V8". Journal of Biochemistry. 110 (6): 859–62. PMID 1794975.
  4. ^ Svendsen I, Jensen MR, Breddam K (November 1991). "The primary structure of the glutamic acid-specific protease of Streptomyces griseus". FEBS Letters. 292 (1–2): 165–7. doi:10.1016/0014-5793(91)80859-2. PMID 1959600.
  5. ^ Breddam K, Meldal M (May 1992). "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. doi:10.1111/j.1432-1033.1992.tb16906.x. PMID 1587264.