EC Number   |
General Information |
Reference |
|---|
   4.2.1.150 | 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 |
-, 748646 |
| 4.2.1.150 | 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 |
-, 748646 |
| 4.2.1.150 | 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 |
748646 |
| 4.2.1.150 | more |
both the chromodomain and CoAP domain of CDYL are required for its negative regulation of histone Kcr |
-, 748646 |
| 4.2.1.150 | more |
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 |
-, 746965 |
| 4.2.1.150 | more |
The Mr-Crt catalytic triad is formed by residues Gly120, Glu123 and Glu143 |
-, 748405 |
| 4.2.1.150 | 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 |
-, 748646 |
| 4.2.1.150 | 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 |
748646 |
| 4.2.1.150 | physiological function |
the enzyme catalyzes the dehydration of 3-hydroxybutyryl-CoA to crotonyl-CoA in the n-butanol biosynthetic pathway, molecular mechanism |
-, 746965 |
| 4.2.1.150 | physiological function |
the enzyme is involved in autotrophic carbon fixation |
-, 727751 |
