Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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

Inhibitors

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

Organism

EC Number Organism UniProt Comment Textmining
3.1.1.1 Sulfolobus acidocaldarius Q7M529 fragment
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.1
-
Sulfolobus acidocaldarius

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.1 4-nitrophenyl acetate + H2O
-
Sulfolobus acidocaldarius 4-nitrophenol + acetate
-
?
3.1.1.1 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 ?
-
?