E-mail:gzliang@cqu.edu.cn    Tel: (86)2365102507

Enzyme - EC 3.4.23.1
DFBP ID DFBPENZY0028
EC Number EC 3.4.23.1
Term Pepsin (pH ≥ 2)
Introduction
DFBP ID DFBPENZY0028
EC Number EC 3.4.23.1
Accepted Name

Accepted name:
     • Pepsin A
Alternative name(s):
     • Pepsin

Cleavage sites
Number
Pn------
P4
P3
P2
P1
Cleavage sites
P1'
P2'
------Pm'
site.1------
-
not H, K or Rnot P
not R
-|-F, L, W or Ynot P
------
site.2-------not H, K or Rnot PF, L, W or Y-|--
not P------
Cross-references
Database(s)
ExPASy - ENZYMEEC 3.4.23.1
MEROPS database
Enzyme ID A01.001
ExplorEnz database
EC 3.4.23.1
Reference(s)
Literature(s)

[1] Keil, B. Specificity of proteolysis. Springer-Verlag Berlin-Heidelberg-NewYork, pp.335. (1992)
[2] Keil, B., Tong T.N. LYSIS. Springer-Verlag Berlin-Heidelberg-NewYork, diskette set. (1992)
[3] Lee, D. and Ryle, A.P. Pepsinogen D. A fourth proteolytic zymogen from pig gastric mucosa. Biochem. J. 104 (1967) 735–741. [PMID: 4167464]
[4] Lee, D. and Ryle, A.P. Pepsin D. A minor component of commercial pepsin preparations. Biochem. J. 104 (1967) 742–748. [PMID: 4860638]
[5] Foltmann, R. Gastric proteinases -structure, function, evolution and mechanism of action. Essays Biochem. 17 (1981) 52–84. [PMID: 6795036]
[6] James, M.N.G. and Sielecki, A.R. Molecular structure of an aspartic proteinase zymogen, porcine pepsinogen, at 1.8 Å resolution. Nature 319 (1986) 33–38. [DOI] [PMID: 3941737]
[7] Fruton, J.S. Aspartyl proteinases.  In: Neuberger, A. and Brocklehurst, K. (Ed.), New Comprehensive Biochemistry: Hydrolytic Enzymes, vol. 16, Elsevier, Amsterdam, 1987, pp. 1–38.
[8] Tang, J. and Wong, R.N.S. Evolution in the structure and function of aspartic proteases. J. Cell. Biochem. 33 (1987) 53–63. [DOI] [PMID: 3546346]
[9] Pohl, J. and Dunn, B.M. Secondary enzyme-substrate interactions: kinetic evidence for ionic interactions between substrate side chains and the pepsin active site. Biochemistry 27 (1988) 4827–4834. [PMID: 3139029]

Copyright © 2020. Record / license number: Chongqing ICP No. 2000214