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Enoyl-CoA Hydratase
Known as:
Crotonase
, trans-2-Enoyl-Coenzyme A Hydratase
, Enoyl CoA Hydratases
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An enzyme that catalyzes reversibly the hydration of unsaturated fatty acyl-CoA to yield beta-hydroxyacyl-CoA. It plays a role in the oxidation of…
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National Institutes of Health
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Related topics
Related topics
15 relations
Narrower (5)
AUH protein, human
HACL1 protein, human
PaaF protein, E coli
PaaG protein, E coli
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ECH1 gene
ECHDC1 gene
ECHS1 gene
In Blood
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Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
1999
1999
Mutagenic and enzymological studies of the hydratase and isomerase activities of 2-enoyl-CoA hydratase-1.
T. Kiema
,
Christian K. Engel
,
Werner Schmitz
,
S. Filppula
,
Rik K. Wierenga
,
J. Hiltunen
Biochemistry
1999
Corpus ID: 24113905
Structural and enzymological studies have shown the importance of Glu144 and Glu164 for the catalysis by 2-enoyl-CoA hydratase-1…
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Highly Cited
1998
Highly Cited
1998
2-Ketocyclohexanecarboxyl Coenzyme A Hydrolase, the Ring Cleavage Enzyme Required for Anaerobic Benzoate Degradation byRhodopseudomonas palustris
D. Pelletier
,
C. Harwood
Journal of Bacteriology
1998
Corpus ID: 32692940
ABSTRACT 2-Ketocyclohexanecarboxyl coenzyme A (2-ketochc-CoA) hydrolase has been proposed to catalyze an unusual hydrolytic ring…
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Highly Cited
1998
Highly Cited
1998
Effect of Carboxamido N Coordination to Iron on the Redox Potential of Low-Spin Non-Heme Iron Centers with N,S Coordination: Relevance to the Iron Site of Nitrile Hydratase.
J. Noveron
,
M. Olmstead
,
P. Mascharak
Inorganic Chemistry
1998
Corpus ID: 41462517
The redox parameters of [Fe(PyPepS)2]-, the first low-spin Fe(III) complex with both carboxamido N and thiolato S donors in the…
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Review
1998
Review
1998
Biotransformation of nitriles by rhodococci
A. Bunch
Antonie van Leeuwenhoek
1998
Corpus ID: 36945847
Rhodococci have been shown to be capable of a very wide range of biotransformations. Of these, the conversion of nitriles into…
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Highly Cited
1991
Highly Cited
1991
Nucleotide sequence of the promoter and fadB gene of the fadBA operon and primary structure of the multifunctional fatty acid oxidation protein from Escherichia coli.
X. Y. Yang
,
H. Schulz
,
M. Elzinga
,
S. Yang
Biochemistry
1991
Corpus ID: 20697263
The primary structure of a multifunctional protein, the large alpha-subunit of the Escherichia coli fatty acid oxidation complex…
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Highly Cited
1982
Highly Cited
1982
Immunocytochemical localization of catalase and heat-labile enoyl-CoA hydratase in the livers of normal and peroxisome proliferator-treated rats.
M. Bendayan
,
J. Reddy
Laboratory investigation; a journal of technical…
1982
Corpus ID: 21601998
The intracellular localization of catalase and the heat-labile enoyl-CoA hydratase (second enzyme of the peroxisomal fatty acid…
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1980
1980
A bifunctional enzyme from glyoxysomes. Purification of a protein possessing enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase activities.
J. Frevert
,
H. Kindl
European Journal of Biochemistry
1980
Corpus ID: 42734719
1. Enoyl-CoA hydratase and 3-hydroxyacyl-CoA dehydrogenase copurified when extracts from cotyledons of 5-day-old cucumber…
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Highly Cited
1977
Highly Cited
1977
Purification and properties of pig heart crotonase and the presence of short chain and long chain enoyl coenzyme A hydratases in pig and guinea pig tissues.
J. Fong
,
H. Schulz
Journal of Biological Chemistry
1977
Corpus ID: 24646314
A short chain enoyl-CoA hydratase (crotonase) from pig heart has been purified to apparent homogeneity. The enzyme has an…
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Highly Cited
1975
Highly Cited
1975
Substrate stereochemistry of the enoyl-CoA hydratase reaction.
P. Willadsen
,
H. Eggerer
European Journal of Biochemistry
1975
Corpus ID: 21570223
1. A specimen of stereospecifically 2-tritiated 3-hydroxybutyric acid was prepared by hydroboration of ethyl crotonate. It was…
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Highly Cited
1973
Highly Cited
1973
LOCALIZATION OF ENZYMES WITHIN MICROBODIES
A. Huang
,
H. Beevers
Journal of Cell Biology
1973
Corpus ID: 15731199
Microbodies from rat liver and a variety of plant tissues were osmotically shocked and subsequently centrifuged at 40,000 g for…
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