3.4.23.28: Acrocylindropepsin

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

Word Map on EC 3.4.23.28

3.4.23.28

3.4.23.6

proteinases

r-factors

endothiapepsin

renin

rhizopuspepsin

pepstatin

rhizopus

beta-hairpins

root-mean-square

scissile

hydroxyethylene

non-hydrogen

penicillopepsin

statine-containing

Reaction

Preference for hydrophobic residues at P1 and P1'. Action on the B chain of insulin is generally similar to that of pepsin A, but it also cleaves Leu6-/-Cys(SO3H), Glu21-/-Arg and Asn3-/-Gln, although not Gln4-His =

Synonyms

Acrocylindricum proteinase, Acrocylindrium acid proteinase, Acrocylindrium proteinase, EC 3.4.23.6, EC 3.4.4.17, EC 3.4.99.1, More, Proteinase, Acrocylindricum

ECTree

3 Hydrolases

3.4 Acting on peptide bonds (peptidases)

3.4.23 Aspartic endopeptidases

3.4.23.28 Acrocylindropepsin

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Results	in table
7	AA Sequence
1	CAS Registry Number
2	Crystallization (Commentary)
6	Inhibitors
1	Localization
3	Natural Substrates/ Products (Substrates)
3	Organism
1	pH Optimum
1	pH Stability
1	Purification (Commentary)
1	Reaction
1	Reaction Type
3	Reference
1	Specific Activity [micromol/min/mg]
8	Substrates and Products (Substrate)
8	Synonyms
1	Temperature Optimum [°C]
2	Temperature Stability [°C]

Reference

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Reference on EC 3.4.23.28 - Acrocylindropepsin

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30568

Takahashi, K.; Chang, W.J.

The structure and function of acid proteases. V. Comparative studies on the specific inhibition of acid proteases by diazoacetyl-DL-norleucine methyl ester, 1,2-epoxy-3-(p-nitrophenoxy) propane and pepstatin

J. Biochem.

497-506

1976

Acrocylindrium sp.

10290

30726

Ichihara, S.; Uchino, F.

Specificity of acid proteinase from Acrocylindrium

Agric. Biol. Chem.

423-428

1975

Acrocylindrium sp.

668811

Takahashi, K.

Acrocylindropepsin

Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )

91-92

2004

Acrocylindrium sp.