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Literature summary for 3.4.23.42 extracted from

  • Fusek, M.; Lin, X.L.; Tang, J.
    Enzymic properties of thermopsin (1990), J. Biol. Chem., 265, 1496-1501.
    View publication on PubMed
Search for more literature for 3.4.23.42

Inhibitors

Inhibitors Comment Organism Structure
1,2-epoxy-3-(p-nitrophenoxy)propane
-
 Sulfolobus acidocaldarius
acetamide
-
 Sulfolobus acidocaldarius
diazoacetyl-DL-norleucine
-
 Sulfolobus acidocaldarius
HgCl2 reversible by 2-mercaptoethanol Sulfolobus acidocaldarius
pepstatin
-
 Sulfolobus acidocaldarius
phenylalaninamide
-
 Sulfolobus acidocaldarius
Urea
-
 Sulfolobus acidocaldarius

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.053
-
 Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Ala-Leu
-
 Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius
-
-
-

Reaction

Reaction Comment Organism Reaction ID
similar in specificity to pepsin A preferring bulky hydrophobic amino acids in P1 and P1' prefers large hydrophobic residues at both sides of the scissile bond Sulfolobus acidocaldarius
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Bovine serum albumin + H2O
-
 Sulfolobus acidocaldarius ?
-
 ?
glyceraldehyde-3-phosphate dehydrogenase + H2O
-
 Sulfolobus acidocaldarius ?
-
 ?
Hemoglobin + H2O
-
 Sulfolobus acidocaldarius ?
-
 ?
Lys-Pro-Ala-Glu-Phe-(4-nitro)Phe-Ala-Leu + H2O
-
 Sulfolobus acidocaldarius Lys-Pro-Ala-Glu-Phe + (4-nitro)Phe-Ala-Leu
-
 ?
ovalbumin + H2O
-
 Sulfolobus acidocaldarius ?
-
 ?
oxidized insulin B + H2O following bonds are hydrolyzed: Leu-Val, Leu-Tyr, Phe-Phe, Phe-Tyr, Tyr-Thr Sulfolobus acidocaldarius ?
-
 ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
75
-
-
 Sulfolobus acidocaldarius

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
2
-
-
 Sulfolobus acidocaldarius