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Literature summary for 3.4.23.42 extracted from

  • Lin, X.; Fusek, M.; Tang, J.
    Thermopsin, a thermostable acid protease from Sulfolobus acidocaldarius (1991), Adv. Exp. Med. Biol., 306, 255-257.
    View publication on PubMed
Search for more literature for 3.4.23.42

Cloned(Commentary)

Cloned (Comment) Organism
-
 Sulfolobus acidocaldarius

Inhibitors

Inhibitors Comment Organism Structure
1,2-epoxy-3-(p-nitrophenoxy)propane
-
 Sulfolobus acidocaldarius
diazoacetyl-DL-norleucine
-
 Sulfolobus acidocaldarius
Hg(CH3COO)2
-
 Sulfolobus acidocaldarius
pepstatin
-
 Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
side-chain modification glycoprotein Sulfolobus acidocaldarius

Purification (Commentary)

Purification (Comment) Organism
-
 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.
additional information The characteristic active site amino acid sequence for aspartic proteases, Asp Thr Gly, which is present in all aspartic proteases even with only distant evolutionary relatedness, is absent in thermopsin from Sulfolobus acidocaldarius, suggesting that a different catalytic mechanisms is employed. Sulfolobus acidocaldarius ?
-
 ?

pH Optimum

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