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Information on EC 4.2.1.150 - short-chain-enoyl-CoA hydratase and Organism(s) Homo sapiens and UniProt Accession Q9Y232

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EC Tree
     4 Lyases
         4.2 Carbon-oxygen lyases
             4.2.1 Hydro-lyases
                4.2.1.150 short-chain-enoyl-CoA hydratase
IUBMB 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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Homo sapiens
UNIPROT: Q9Y232
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The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
chromodomain y-like protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
chromodomain Y-like protein
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crotonyl-CoA hydratase
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additional information
cf. EC 4.2.1.17
PATHWAY SOURCE
PATHWAYS
-
-, -, -, -, -, -, -, -, -, -, -, -, -
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
crotonyl-CoA + H2O
3-hydroxybutyryl-CoA
show the reaction diagram
-
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
crotonyl-CoA + H2O
3-hydroxybutyryl-CoA
show the reaction diagram
-
-
-
r
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
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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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
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
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
additional information
both the chromodomain and CoAP domain of CDYL are required for its negative regulation of histone Kcr
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CDYL_HUMAN
598
0
66482
Swiss-Prot
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Homo sapiens (Q9Y232), Mus musculus (Q9WTK2), Mus musculus C57BL/6 (Q9WTK2)
Manually annotated by BRENDA team