Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase

Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase

Item
http://www.wikidata.org/entity/Q27622715
Glutamate 170 of human l-3-hydroxyacyl-CoA dehydrogenase is required for proper orientation of the catalytic histidine and structural integrity of the enzymeThe Multifunctional Protein in Peroxisomal  -Oxidation: STRUCTURE AND SUBSTRATE SPECIFICITY OF THE ARABIDOPSIS THALIANA PROTEIN MFP2Crystal Structure of Liganded Rat Peroxisomal Multifunctional Enzyme Type 1: A FLEXIBLE MOLECULE WITH TWO INTERCONNECTED ACTIVE SITESMolecular differences between a mutase and a phosphatase: investigations of the activation step in Bacillus cereus phosphopentomutase.Purification, crystallization and preliminary crystallographic analysis of 3-hydroxyacyl-CoA dehydrogenase fromCaenorhabditis elegansStructural modelling and comparative analysis of homologous, analogous and specific proteins from Trypanosoma cruzi versus Homo sapiens: putative drug targets for chagas' disease treatment.Dimerization interface of 3-hydroxyacyl-CoA dehydrogenase tunes the formation of its catalytic intermediate.Crystallization and preliminary X-ray crystallographic analysis of rabbit L-gulonate 3-dehydrogenase.Cloning, expression, purification, crystallization and X-ray crystallographic analysis of (S)-3-hydroxybutyryl-CoA dehydrogenase from Clostridium butyricum.A structurally conserved water molecule in Rossmann dinucleotide-binding domains.Structural basis for channelling mechanism of a fatty acid beta-oxidation multienzyme complex5-Hydroxydecanoate is metabolised in mitochondria and creates a rate-limiting bottleneck for beta-oxidation of fatty acids.Structural enzymology comparisons of multifunctional enzyme, type-1 (MFE1): the flexibility of its dehydrogenase part.
P2860

Sequestration of the active site by interdomain shifting. Crystallographic and spectroscopic evidence for distinct conformations of L-3-hydroxyacyl-CoA dehydrogenase

Item
http://www.wikidata.org/entity/Q27622715
description
2000 nî lūn-bûn
@nan
2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Sequestration of the active si ...... -hydroxyacyl-CoA dehydrogenase
@ast
Sequestration of the active si ...... -hydroxyacyl-CoA dehydrogenase
@en
Sequestration of the active si ...... -hydroxyacyl-CoA dehydrogenase
@nl
type
label
Sequestration of the active si ...... -hydroxyacyl-CoA dehydrogenase
@ast
Sequestration of the active si ...... -hydroxyacyl-CoA dehydrogenase
@en
Sequestration of the active si ...... -hydroxyacyl-CoA dehydrogenase
@nl
prefLabel
Sequestration of the active si ...... -hydroxyacyl-CoA dehydrogenase
@ast
Sequestration of the active si ...... -hydroxyacyl-CoA dehydrogenase
@en
Sequestration of the active si ...... -hydroxyacyl-CoA dehydrogenase
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P698
P356
P1433
P1476
Sequestration of the active si ...... -hydroxyacyl-CoA dehydrogenase
@en
P2093
P304
P31
P356
P407
P433
P478
P577
P698