Type | Description |
---|---|
Definition | malonyl-CoA decarboxylase |
Date | Results | Publications |
---|---|---|
2017-04-29 10:13:00 | To identify the active site of MCD, molecular docking and molecular dynamics simulations were performed to explore the interactions of human mitochondrial MCD (HmMCD) and CoA derivatives. The findings reveal that the active site of HmMCD indeed resides in the prominent groove which resembles that of curacin A. | 26948533 |
2017-01-14 10:52:00 | Our result expands the phenotype of malonyl-CoA decarboxylase deficiency and suggests attentions should be paid to the mild form of disorders, for example, malonyl-CoA decarboxylase deficiency, which usually present a severe disease course. | 26858006 |
2014-02-08 10:47:00 | The MLYCD catalytic domain is structurally homologous to those of the GCN5-related N-acetyltransferase superfamily. | 23791943 |
2013-06-29 12:27:00 | Structural asymmetry and disulfide bridges among subunits modulate the activity of human malonyl-CoA decarboxylase. | 23482565 |
2012-10-13 10:38:00 | Our case emphasizes the need for ongoing cardiac disease screening in patients with MCD deficiency and the benefits and limitations of current dietary interventions. | 22778304 |
Type | IDs |
---|---|
Synonymous | MCD |
Gene |
UniProtKB-ID:
DCMC_HUMAN
UniprotKB:
O95822
UniParc:
UPI000013D2B1,
UPI0000128FD5
EMBL:
AF090834,
AC009119,
AF153679,
AF097832,
BC000286,
BC052592
Ensembl:
ENSG00000103150
KO:
hsa:23417
|
Nucleutide sequences |
EMBL-CDS:
AAH00286.1,
AAH52592.1,
AAD16177.2,
AAD48994.1,
AAD34631.1
Ensembl_TRS:
ENST00000262430
|
Protein sequencees |
Ensembl_PRO:
ENSP00000262430
RefSeq:
NP_036345.2
|
Others |
UniRef100:
UniRef100_O95822
UniRef90:
UniRef90_O95822
UniRef50:
UniRef50_O95822
UniGene:
Hs.644610
CCDS:
CCDS42206.1
|
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Refseq |
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