Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme

Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme

Item
http://www.wikidata.org/entity/Q27633168
The Multifunctional Protein in Peroxisomal  -Oxidation: STRUCTURE AND SUBSTRATE SPECIFICITY OF THE ARABIDOPSIS THALIANA PROTEIN MFP2The isomerase and hydratase reaction mechanism of the crotonase active site of the multifunctional enzyme (type-1), as deduced from structures of complexes with 3S-hydroxy-acyl-CoAA single amino acid change (substitution of the conserved Glu-590 with alanine) in the C-terminal domain of rat liver carnitine palmitoyltransferase I increases its malonyl-CoA sensitivity close to that observed with the muscle isoform of the enzymeIdentification by mutagenesis of a conserved glutamate (Glu487) residue important for catalytic activity in rat liver carnitine palmitoyltransferase IIIdentification by mutagenesis of conserved arginine and glutamate residues in the C-terminal domain of rat liver carnitine palmitoyltransferase I that are important for catalytic activity and malonyl-CoA sensitivityCrystallization and preliminary X-ray crystallographic analysis of rabbit L-gulonate 3-dehydrogenase.Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complexAlanine-scanning mutation approach for classification of the roles of conserved residues in the activity and substrate affinity of L-carnitine dehydrogenase.Structural enzymology comparisons of multifunctional enzyme, type-1 (MFE1): the flexibility of its dehydrogenase part.Role of 3-Hydroxy Fatty Acid-Induced Hepatic Lipotoxicity in Acute Fatty Liver of Pregnancy.Rat liver carnitine palmitoyltransferase 1 forms an oligomeric complex within the outer mitochondrial membrane.Identification of residues essential for the activity and substrate affinity of L-carnitine dehydrogenase.Cryo-EM structure of human mitochondrial trifunctional protein
P2860

Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzyme

Item
http://www.wikidata.org/entity/Q27633168
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Glutamate 170 of human l-3-hyd ...... ctural integrity of the enzyme
@ast
Glutamate 170 of human l-3-hyd ...... ctural integrity of the enzyme
@en
Glutamate 170 of human l-3-hyd ...... ctural integrity of the enzyme
@nl
type
label
Glutamate 170 of human l-3-hyd ...... ctural integrity of the enzyme
@ast
Glutamate 170 of human l-3-hyd ...... ctural integrity of the enzyme
@en
Glutamate 170 of human l-3-hyd ...... ctural integrity of the enzyme
@nl
prefLabel
Glutamate 170 of human l-3-hyd ...... ctural integrity of the enzyme
@ast
Glutamate 170 of human l-3-hyd ...... ctural integrity of the enzyme
@en
Glutamate 170 of human l-3-hyd ...... ctural integrity of the enzyme
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Glutamate 170 of human l-3-hyd ...... ctural integrity of the enzyme
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P698