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Literature summary for 3.1.1.1 extracted from

  • Sobek, H.; G๖risch, H.
    Further kinetic and molecular characterization of an extremely heat-stable carboxylesterase from the thermoacidophilic archaebacterium Sulfolobus acidocaldarius. (1989), Biochem. J., 261, 993-998.
    View publication on PubMedView publication on EuropePMC
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Inhibitors

Inhibitors Comment Organism Structure
butan-1-ol 27 mM, complete inhibition Sulfolobus acidocaldarius
Diethyl p-nitrophenyl phosphate
-
 Sulfolobus acidocaldarius
propan-1-ol
-
 Sulfolobus acidocaldarius
propan-2-ol weaker effect than propan-1-ol Sulfolobus acidocaldarius

Organism

Organism UniProt Comment Textmining
Sulfolobus acidocaldarius Q7M529 fragment
-

Purification (Commentary)

Purification (Comment) Organism
-
 Sulfolobus acidocaldarius

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-nitrophenyl acetate + H2O
-
 Sulfolobus acidocaldarius 4-nitrophenol + acetate
-
 ?
additional information esterase-catalysed transesterification of p-nitrophenyl acetate by reaction with alcohol as nucleophile. The enzyme catalyses an acyl-group transfer with triacetin as acyl donor and aniline as acyl acceptor Sulfolobus acidocaldarius ?
-
 ?