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Information on EC 4.2.1.150 - short-chain-enoyl-CoA hydratase
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4.2.1.150 short-chain-enoyl-CoA hydrataseIUBMB Comments
The enzyme from the bacterium Clostridium acetobutylicum is part of the central fermentation pathway and plays a key role in the production of both acids and solvents. It is specific for short, C4-C6, chain length substrates and exhibits an extremely high turnover number for crotonyl-CoA. cf. EC 4.2.1.17, enoyl-CoA hydratase and EC 4.2.1.74, long-chain-enoyl-CoA hydratase.
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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Reaction Schemes
Synonyms
chromodomain y-like protein, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CaCRT
CDYL
chromodomain Y-like protein
crotonase
crotonyl-CoA hydratase
Mr-Crt
Mrub_2284
Msed_0399
additional information
Msed_0399
locus name, bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
Msed_0399
locus name, bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a short-chain (3S)-3-hydroxyacyl-CoA = a short-chain trans-2-enoyl-CoA + H2O
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-
-
-
a short-chain (3S)-3-hydroxyacyl-CoA = a short-chain trans-2-enoyl-CoA + H2O
the Mr-Crt catalytic mechanism constitutes a concerted attack by the two glutamate residues. While Glu143 of Mr-Crt protonates the substrate, Glu123 abstracts a proton from a bound water molecule. The Gly120 activates the substrate by a hydrogen bond to the oxygen of the enoyl moiety of the CoA ester. The binding pocket for the CoA moiety is formed by characteristic hydrophobic amino acids and lysine residues
a short-chain (3S)-3-hydroxyacyl-CoA = a short-chain trans-2-enoyl-CoA + H2O
the Mr-Crt catalytic mechanism constitutes a concerted attack by the two glutamate residues. While Glu143 of Mr-Crt protonates the substrate, Glu123 abstracts a proton from a bound water molecule. The Gly120 activates the substrate by a hydrogen bond to the oxygen of the enoyl moiety of the CoA ester. The binding pocket for the CoA moiety is formed by characteristic hydrophobic amino acids and lysine residues
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PATHWAY SOURCE
PATHWAYS
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, CO2 fixation in Crenarchaeota, CO2 fixation in Crenarchaeota, CO2 fixation in Crenarchaeota, CO2 fixation in Crenarchaeota, CO2 fixation in Crenarchaeota, CO2 fixation in Crenarchaeota, CO2 fixation in Crenarchaeota, CO2 fixation in Crenarchaeota, CO2 fixation in Crenarchaeota, CO2 fixation in Crenarchaeota, CO2 fixation in Crenarchaeota, CO2 fixation in Crenarchaeota
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SYSTEMATIC NAME
IUBMB Comments
short-chain-(3S)-3-hydroxyacyl-CoA hydro-lyase
The enzyme from the bacterium Clostridium acetobutylicum is part of the central fermentation pathway and plays a key role in the production of both acids and solvents. It is specific for short, C4-C6, chain length substrates and exhibits an extremely high turnover number for crotonyl-CoA. cf. EC 4.2.1.17, enoyl-CoA hydratase and EC 4.2.1.74, long-chain-enoyl-CoA hydratase.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
a short-chain trans-2-enoyl-CoA + H2O
short-chain (3S)-3-hydroxyacyl-CoA
-
the enzyme is specific for short chain fatty acyl-CoA substrates and is sensitive to high concentrations of crotonyl-CoA. It requires a complete coenzyme A thioester substrate for efficient catalysis
-
-
?
3-hydroxybutyryl-CoA
crotonyl-CoA + H2O
Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
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-
-
r
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in autotrophic carbon fixation
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-
?
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
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-
?
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
-
-
?
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
bifunctional crotonyl-CoA hydratase/(S)-3-hydroxybutanoyl-CoA dehydrogenase (EC 4.2.1.150/EC 1.1.1.35)
-
-
?
additional information
?
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enzyme residues Ser69 and Ala24 are signature residues of CaCRT, resulting in a distinct ADP binding mode wherein the ADP moiety of acetoacetyl-CoA is bound at a different position compared with other crotonases. The substrate specificity of crotonase enzymes is determined by both the structural feature of the a3 helix region and the residues contributing the enoyl-CoA binding pocket. A tight formed a3 helix and two phenylalanine residues, Phe143 and Phe233, aid CaCRT to accommodate crotonyl-CoA as the substrate. Phe143 and Phe233 are key residues for the constitution of the crotonyl binding pocket to accommodate the four-carbon crotonyl-CoA as a substrate
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-
?
additional information
?
-
Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
enzyme residues Ser69 and Ala24 are signature residues of CaCRT, resulting in a distinct ADP binding mode wherein the ADP moiety of acetoacetyl-CoA is bound at a different position compared with other crotonases. The substrate specificity of crotonase enzymes is determined by both the structural feature of the a3 helix region and the residues contributing the enoyl-CoA binding pocket. A tight formed a3 helix and two phenylalanine residues, Phe143 and Phe233, aid CaCRT to accommodate crotonyl-CoA as the substrate. Phe143 and Phe233 are key residues for the constitution of the crotonyl binding pocket to accommodate the four-carbon crotonyl-CoA as a substrate
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
-
?
crotonyl-CoA + H2O
(S)-3-hydroxybutanoyl-CoA
the enzyme is involved in autotrophic carbon fixation
-
-
?
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
crotonyl-CoA
-
the enzyme is markedly sensitive to inhibition by crotonyl-CoA at concentrations greater than about 0.075 mM
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Carcinoma, Hepatocellular
Circular RNA hsa_circ_0008285 inhibits colorectal cancer cell proliferation and migration via the miR-382-5p/PTEN axis.
Lymphoma
Circular RNA hsa_circ_0008285 inhibits colorectal cancer cell proliferation and migration via the miR-382-5p/PTEN axis.
Lymphoma, Mantle-Cell
Circular RNA hsa_circ_0008285 inhibits colorectal cancer cell proliferation and migration via the miR-382-5p/PTEN axis.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
steady-state kinetics of the CDYL-catalyzed hydratation reaction compared to mitochondrial metabolic enzyme enoyl-CoA hydratase (ECH, EC 4.2.1.17) as a positive control
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 8
pH 8.0, 65°C, native enzyme, autotrophically- or heterotrophically-grown cell
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 78
activity range, 20% of maximal activity at 30°C, 60% at 75°C, over 80% at 50-70°C, and maximal activity at 55°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
the C-terminal CoAP domain of the CDY family proteins including CDYL has a three-dimensional structure closely resembling enoyl-CoA hydratase, which catalyzes the hydratation of 2-trans-enoyl-CoA into beta-hydroxyacyl-CoA in mitochondria during beta-oxidation of fatty acids
evolution
the C-terminal CoAP domain of the CDY family proteins including CDYL has a three-dimensional structure closely resembling enoyl-CoA hydratase, which catalyzes the hydratation of 2-trans-enoyl-CoA into beta-hydroxyacyl-CoA in mitochondria during beta-oxidation of fatty acids
evolution
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the C-terminal CoAP domain of the CDY family proteins including CDYL has a three-dimensional structure closely resembling enoyl-CoA hydratase, which catalyzes the hydratation of 2-trans-enoyl-CoA into beta-hydroxyacyl-CoA in mitochondria during beta-oxidation of fatty acids
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malfunction
Cdyl knockout mice are embryonically lethal or died shortly after birth with significantly reduced levels of histone Kcr in elongating spermatids from Cdyl transgenic mice compared to that from wild-type mice, although the level of histone acetylation is comparable
malfunction
the levels of total histone Kcr and H2BK12cr on the promoter of known CDYL target genes BDNF, NEUROD1, SCG10, and MYT1 increase significantly in CDYL-KO HeLa cells, whereas the regional level of H3K27me3 in these cells decreases, expression patterns, overview
malfunction
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Cdyl knockout mice are embryonically lethal or died shortly after birth with significantly reduced levels of histone Kcr in elongating spermatids from Cdyl transgenic mice compared to that from wild-type mice, although the level of histone acetylation is comparable
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physiological function
the enzyme is involved in autotrophic carbon fixation
physiological function
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
physiological function
the chromodomain Y-like protein CDYL acts as a crotonyl-CoA hydratase to negatively regulate histone crotonylation. The chromodomain Y-like transcription corepressor CDYL negatively regulates histone Kcr by acting as a crotonyl-CoA hydratase to convert crotonyl-CoA to beta-hydroxybutyryl-CoA. This activity is intrinsically linked to the transcription repression function of CDYL and is implemented in reactivation of sex chromosome-linked genes and histone replacement during spermatogenesis. The negative regulation of histone Kcr by CDYL is intrinsically linked to its transcription repression activity and functionally implemented in the reactivation of sex chromosome-linked genes in round spermatids and genome-wide histone replacement in elongating spermatids
physiological function
the chromodomain Y-like protein CDYL acts as a crotonyl-CoA hydratase to negatively regulate histone crotonylation. The chromodomain Y-like transcription corepressor CDYL negatively regulates histone Kcr by acting as a crotonyl-CoA hydratase to convert crotonyl-CoA to beta-hydroxybutyryl-CoA. This activity is intrinsically linked to the transcription repression function of CDYL and is implemented in reactivation of sex chromosome-linked genes and histone replacement during spermatogenesis. The negative regulation of histone Kcr by CDYL is intrinsically linked to its transcription repression activity and functionally implemented in the reactivation of sex chromosome-linked genes in round spermatids and genome-wide histone replacement in elongating spermatids. Cdyl regulates the expression of sex chromosome-linked escaped genes in postmeiotic spermatogenic cells by mainly influencing histone Kcr on the gene promoters. The enzyme is important in the physiology of male reproduction and the mechanism of the spermatogenic failure in AZFc (azoospermia factor c)-deleted infertile men
physiological function
the enzyme catalyzes the dehydration of 3-hydroxybutyryl-CoA to crotonyl-CoA in the n-butanol biosynthetic pathway, molecular mechanism
physiological function
-
the chromodomain Y-like protein CDYL acts as a crotonyl-CoA hydratase to negatively regulate histone crotonylation. The chromodomain Y-like transcription corepressor CDYL negatively regulates histone Kcr by acting as a crotonyl-CoA hydratase to convert crotonyl-CoA to beta-hydroxybutyryl-CoA. This activity is intrinsically linked to the transcription repression function of CDYL and is implemented in reactivation of sex chromosome-linked genes and histone replacement during spermatogenesis. The negative regulation of histone Kcr by CDYL is intrinsically linked to its transcription repression activity and functionally implemented in the reactivation of sex chromosome-linked genes in round spermatids and genome-wide histone replacement in elongating spermatids
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physiological function
-
the enzyme is involved in the 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
-
physiological function
-
the enzyme is involved in autotrophic carbon fixation
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physiological function
Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
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the enzyme catalyzes the dehydration of 3-hydroxybutyryl-CoA to crotonyl-CoA in the n-butanol biosynthetic pathway, molecular mechanism
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additional information
both the chromodomain and CoAP domain of CDYL are required for its negative regulation of histone Kcr
additional information
both the chromodomain and CoAP domain of CDYL are required for its negative regulation of histone Kcr
additional information
substrate binding pocket structure and mechanism, overview. CaCRT uses a unique CoA binding mode. The Ser69 residue in CaCRT is hydrogen-bonded with N6 of AcAc-CoA, in contrast to the corresponding Lys101 and Val74 residues in ECH and DmdD, and is involved in the stabilization of the adenine ring. Moreover, Ala24 of CaCRT is located near the phosphate moiety, whereas the corresponding Lys31 residue of DmdD is hydrogen-bonded with this moiety
additional information
The Mr-Crt catalytic triad is formed by residues Gly120, Glu123 and Glu143
additional information
-
both the chromodomain and CoAP domain of CDYL are required for its negative regulation of histone Kcr
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additional information
-
The Mr-Crt catalytic triad is formed by residues Gly120, Glu123 and Glu143
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additional information
Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
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substrate binding pocket structure and mechanism, overview. CaCRT uses a unique CoA binding mode. The Ser69 residue in CaCRT is hydrogen-bonded with N6 of AcAc-CoA, in contrast to the corresponding Lys101 and Val74 residues in ECH and DmdD, and is involved in the stabilization of the adenine ring. Moreover, Ala24 of CaCRT is located near the phosphate moiety, whereas the corresponding Lys31 residue of DmdD is hydrogen-bonded with this moiety
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Show AA Sequence and Transmembrane Helices (1124 entries)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
158000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexamer
homotetramer
additional information
hexamer
Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
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a dimer of trimers
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additional information
the CaCRT monomer consists of an N-terminal (NTD) and a C-terminal domain (CTD). The NTD (beta1-beta7 and alpha1-alpha9) harbors the canonical crotonase fold, where a large beta-sheet (beta1-beta4 and beta6) is organized with a small beta-sheet (beta5 and beta7) forming two perpendicular beta-sheets. The CTD consists of three alpha-helices (alpha10-alpha12), and this domain mediates the oligomerization of CaCRT. Additionally, the extended alpha-helix (alpha12) interacts with the NTD of a neighboring monomer and participates in the formation of its substrate binding site. The CTDs of six monomers participate mainly in the formation of the hexameric interface
additional information
Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
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the CaCRT monomer consists of an N-terminal (NTD) and a C-terminal domain (CTD). The NTD (beta1-beta7 and alpha1-alpha9) harbors the canonical crotonase fold, where a large beta-sheet (beta1-beta4 and beta6) is organized with a small beta-sheet (beta5 and beta7) forming two perpendicular beta-sheets. The CTD consists of three alpha-helices (alpha10-alpha12), and this domain mediates the oligomerization of CaCRT. Additionally, the extended alpha-helix (alpha12) interacts with the NTD of a neighboring monomer and participates in the formation of its substrate binding site. The CTDs of six monomers participate mainly in the formation of the hexameric interface
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged enzyme in apo- and acetoacetyl-CoA bound forms, from precipitant solution containing 30% PEG 400, 0.1 M sodium cacodylate, pH 6.5, and 0.2 M lithium sulfate, 22°C, 5 days, X-ray diffraction structure determination and analysis at 2.0-2.2 A resolution, molecular replacement and modelling
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F82A
site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
F143A
Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
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site-directed mutagenesis, almost inactive mutant
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F233A
Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
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site-directed mutagenesis, almost inactive mutant
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F82A
Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787
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site-directed mutagenesis, the mutant shows similar activity compared to wild-type enzyme
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additional information
additional information
generation of Cdyl transgenic mice by microinjection of a Cdyl construct into the pro-nuclei of fertilized oocytes, derived from intercross of C57BL/6 3 CBA F1 mice
additional information
-
generation of Cdyl transgenic mice by microinjection of a Cdyl construct into the pro-nuclei of fertilized oocytes, derived from intercross of C57BL/6 3 CBA F1 mice
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
the purified recombinant His-tagged enzyme Mr-Crt displays an extended half-life of over 1 month, IT50: 743 h
50 - 70
purified recombinant His-tagged enzyme, 80% activity remaining after 5 min
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Butanol
Butanol
inhibits the enzyme activity, 45% inhibition at 2% v/v, 80% at 8% v/v
Butanol
-
inhibits the enzyme activity, 45% inhibition at 2% v/v, 80% at 8% v/v
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
acetone precipitation, Sephadex G-200 gel filtration, and DEAE-Sephadex column chromatography
-
recombinant C-terminally His6-tagged wild-type and mutant enzymes from Escherichia coli strain B834 by nickel affinity chromatography and gel filtration
recombinant His-tagged enzyme from Escherichia coli strain Rosetta (DE3) by nickel affinity chromatography and desalting gel filtration
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene Mrub_2284, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain Rosetta (DE3), subcloning in Escherichia coli strain XL-1 Blue
the CaCRT coding gene (Met1-Arg261) is amplified by PCR using the chromosomal DNA of Clostridium acetobutylicum strain ATCC 824 as a template, recombinant expression of C-terminally His6-tagged wild-type and mutant enzymes in Escherichia coli strain B834
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Scherf, U.; Buckel, W.
Purification and properties of an iron-sulfur and FAD-containing 4-hydroxybutyryl-CoA dehydratase/vinylacetyl-CoA DELTA3-DELTA2-isomerase from Clostridium aminobutyricum
Eur. J. Biochem.
215
421-429
1993
Clostridium aminobutyricum
brenda
Waterson, R.M.; Conway, R.S.
Enoyl-CoA hydratases from Clostridium acetobutylicum and Escherichia coli
Methods Enzymol.
71
421-430
1981
Clostridium acetobutylicum
brenda
Waterson, R.M.; Castellino, F.J.; Hass, G.M.; Hill, R.L.
Purification and characterization of cortonase from Clostridium acetobutylicum
J. Biol. Chem.
247
5266-5271
1972
Clostridium acetobutylicum
brenda
Boynton, Z.L.; Bennett, G.N.; Rudolph, F.B.
Cloning, sequencing, and expression of clustered genes encoding beta-hydroxybutyryl-coenzyme A (CoA) dehydrogenase, crotonase, and butyryl-CoA dehydrogenase from Clostridium acetobutylicum ATCC 824
J. Bacteriol.
178
3015-3024
1996
Clostridium acetobutylicum
brenda
Willadsen, P.; Buckel, W.
Assay of 4-hydroxybutyryl-CoA dehydratase from Clostridium aminobutyricum
FEMS Microbiol. Lett.
70
187-191
1990
Clostridium acetobutylicum
brenda
Hawkins, A.B.; Adams, M.W.; Kelly, R.M.
Conversion of 4-hydroxybutyrate to acetyl coenzyme A and its anapleurosis in the Metallosphaera sedula 3-hydroxypropionate/4-hydroxybutyrate carbon fixation pathway
Appl. Environ. Microbiol.
80
2536-2545
2014
Metallosphaera sedula (A4YDS4), Metallosphaera sedula DSM 5348 (A4YDS4)
brenda
Ramos-Vera, W.H.; Weiss, M.; Strittmatter, E.; Kockelkorn, D.; Fuchs, G.
Identification of missing genes and enzymes for autotrophic carbon fixation in crenarchaeota
J. Bacteriol.
193
1201-1211
2011
Metallosphaera sedula (A4YDS4), Metallosphaera sedula DSM 5348 (A4YDS4)
brenda
Kim, E.J.; Kim, Y.J.; Kim, K.J.
Structural insights into substrate specificity of crotonase from the n-butanol producing bacterium Clostridium acetobutylicum
Biochem. Biophys. Res. Commun.
451
431-435
2014
Clostridium acetobutylicum (P52046), Clostridium acetobutylicum ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787 (P52046)
brenda
Reisse, S.; Garbe, D.; Brueck, T.
Identification and characterization of a highly thermostable crotonase from Meiothermus ruber
J. Mol. Catal. B
112
40-44
2015
Meiothermus ruber (D3PLE5), Meiothermus ruber DSM 1279 (D3PLE5)
-
brenda
Liu, S.; Yu, H.; Liu, Y.; Liu, X.; Zhang, Y.; Bu, C.; Yuan, S.; Chen, Z.; Xie, G.; Li, W.; Xu, B.; Yang, J.; He, L.; Jin, T.; Xiong, Y.; Sun, L.; Liu, X.; Han, C.; Cheng, Z.; Liang, J.; Shang, Y.
Chromodomain protein CDYL acts as a crotonyl-CoA hydratase to regulate histone crotonylation and spermatogenesis
Mol. Cell
67
853-866.e5
2017
Mus musculus (Q9WTK2), Homo sapiens (Q9Y232), Mus musculus C57BL/6 (Q9WTK2)
brenda
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