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3.4.23.1: pepsin A

This is an abbreviated version!
For detailed information about pepsin A, go to the full flat file.

Word Map on EC 3.4.23.1

Reaction

Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves Phe1-/-Val, Gln4-/-His, Glu13-/-Ala, Ala14-/-Leu, Leu15-/-Tyr, Tyr16-/-Leu, Gly23-/-Phe, Phe24-/-Phe and Phe25-/-Tyr bonds in the B chain of insulin =

Synonyms

Aspartic proteinase, EC 3.4.4.1, elixir lactate of pepsin, fundus-pepsin, lactated pepsin, lactated pepsin elixir, P I, P-Ia, P-Ib, P-II, P-III, pep/PAG-L, pepsin, pepsin 1, pepsin A, pepsin A1, pepsin A2, pepsin D, pepsin fortior, Pepsin I/II, pepsin R, pepsinogen A, pepsinogen/PAG-Like, pepsins A1, pepsins A2, PG1, PG1-1, PG2, PG2-2, shewasin A, shewasin D

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.1 pepsin A

Crystallization

Crystallization on EC 3.4.23.1 - pepsin A

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystallization in presence of dimethyl sulfoxide. One dimethyl sulfoxide molecule occupies a site on the surface of enzyme interacting with two of its residues. In crystal structure, conformation of enzyme remains unchanged. In solution, dimethyl sulfoxide causes a slight change in secondary structure and complete loss of activity
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hanging-drop vapour diffusion method, crystal structure of the complex between pepsin inhibitor-3 and the enzyme at 1.75 A and at 2.45 A resolution. In the enzyme-inhibitor complex, the N-terminal beta-strand of pepsin inhibitor-3 pairs with one strand of the active site flap (residues 70-82) of pepsin, thus forming an eight-stranded beta-sheet that spans the two proteins
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