Modeling of a mutation responsible for human 3-hydroxy-3-methylglutaryl-CoA lyase deficiency implicates histidine 233 as an active site residue.

Modeling of a mutation responsible for human 3-hydroxy-3-methylglutaryl-CoA lyase deficiency implicates histidine 233 as an active site residue.

Item
http://www.wikidata.org/entity/Q54579333
Characterization of a novel HMG-CoA lyase enzyme with a dual location in endoplasmic reticulum and cytosolCrystal structure of human 3-hydroxy-3-methylglutaryl-CoA Lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduriaInvestigation of conserved acidic residues in 3-hydroxy-3-methylglutaryl-CoA lyase: implications for human disease and for functional roles in a family of related proteinsCharacterization of splice variants of the genes encoding human mitochondrial HMG-CoA lyase and HMG-CoA synthase, the main enzymes of the ketogenesis pathwayHMG CoA lyase deficiency: identification of five causal point mutations in codons 41 and 42, including a frequent Saudi Arabian mutation, R41Q.Influence of multiple cysteines on human 3-hydroxy-3-methylglutaryl-CoA lyase activity and formation of inter-subunit adductsThe 3-hydroxy-methylglutaryl coenzyme A lyase HCL1 is required for macrophage colonization by human fungal pathogen Histoplasma capsulatum.Crystal structures of two bacterial 3-hydroxy-3-methylglutaryl-CoA lyases suggest a common catalytic mechanism among a family of TIM barrel metalloenzymes cleaving carbon-carbon bonds.Structural (betaalpha)8 TIM barrel model of 3-hydroxy-3-methylglutaryl-coenzyme A lyase.Molecular basis of 3-hydroxy-3-methylglutaric aciduria.
P2860

Modeling of a mutation responsible for human 3-hydroxy-3-methylglutaryl-CoA lyase deficiency implicates histidine 233 as an active site residue.

Item
http://www.wikidata.org/entity/Q54579333
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年学术文章
@wuu
1996年学术文章
@zh-cn
1996年学术文章
@zh-hans
1996年学术文章
@zh-my
1996年学术文章
@zh-sg
1996年學術文章
@yue
1996年學術文章
@zh
1996年學術文章
@zh-hant
name
Modeling of a mutation respons ...... 233 as an active site residue.
@en
Modeling of a mutation respons ...... 233 as an active site residue.
@nl
type
label
Modeling of a mutation respons ...... 233 as an active site residue.
@en
Modeling of a mutation respons ...... 233 as an active site residue.
@nl
prefLabel
Modeling of a mutation respons ...... 233 as an active site residue.
@en
Modeling of a mutation respons ...... 233 as an active site residue.
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921
P356
P1433
P1476
Modeling of a mutation respons ...... 233 as an active site residue.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P921