Glutamyl endopeptidase II
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
- ↑ Yoshida, N., Tsuruyama, S., Nagata, K., Hirayama, K., Noda, K. and Makisumi, S. (1988). "Purification and characterization of an acidic amino acid specific endopeptidase of Streptomyces griseus obtained from a commercial preparation (Pronase)". J. Biochem. (Tokyo) 104: 451–456. PMID 3149277.
- ↑ Komiyama, T., Bigler, T.L., Yoshida, N., Noda, K. and Laskowski, M., Jr. (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)". J. Biol. Chem. 266: 10727–10730. PMID 1674942.
- ↑ Nagata, K., Yoshida, N., Ogata, F., Araki, M. and Noda, K. (1991). "Subsite mapping of an acidic amino acid-specific endopeptidase from Streptomyces griseus, GluSGP, and protease V8". J. Biochem. (Tokyo) 110: 859–862. PMID 1794975.
- ↑ Svendsen, I., Jensen, M.R. and Breddam, K. (1991). "The primary structure of the glutamic acid-specific protease of Streptomyces griseus". FEBS Lett. 292: 165–167. doi:10.1016/0014-5793(91)80859-2. PMID 1959600.
- ↑ Breddam, K. and Meldal, M. (1992). "Substrate preferences of glutamic-acid-specific endopeptidases assessed by synthetic peptide substrates based on intramolecular fluorescence quenching". Eur. J. Biochem. 206: 103–107. doi:10.1111/j.1432-1033.1992.tb16906.x. PMID 1587264.
External links
|
---|
| Activity | |
---|
| Regulation | |
---|
| Classification | |
---|
| Types | |
---|
|