ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography

ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography

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http://www.wikidata.org/entity/Q27620927
Identification of the citrate-binding site of human ATP-citrate lyase using X-ray crystallographyBoth subunits of ATP-citrate lyase from Chlorobium tepidum contribute to catalytic activityInvestigation of the catalytic site within the ATP-grasp domain of Clostridium symbiosum pyruvate phosphate dikinaseBiochemical and structural characterization of the GTP-preferring succinyl-CoA synthetase fromThermus aquaticusStructural basis for the binding of succinate to succinyl-CoA synthetaseInteractions of GTP with the ATP-grasp domain of GTP-specific succinyl-CoA synthetaseMitochondrial encephalomyopathy and retinoblastoma explained by compound heterozygosity of SUCLA2 point mutation and 13q14 deletion.Nucleotide recognition in the ATP-grasp protein carbamoyl phosphate synthetaseStructure of NDP-forming Acetyl-CoA synthetase ACD1 reveals a large rearrangement for phosphoryl transfer.Cloning, expression, purification, crystallization and preliminary X-ray analysis of Thermus aquaticus succinyl-CoA synthetaseNovel characteristics of succinate coenzyme A (Succinate-CoA) ligases: conversion of malate to malyl-CoA and CoA-thioester formation of succinate analogues in vitro.Reaction mechanism and structural model of ADP-forming Acetyl-CoA synthetase from the hyperthermophilic archaeon Pyrococcus furiosus: evidence for a second active site histidine residue.Structure of GTP-specific succinyl-CoA synthetase in complex with CoAA positive selection approach identifies residues important for folding of Salmonella enterica Pat, an N(ε)-lysine acetyltransferase that regulates central metabolism enzymes.Kinetic and biochemical analyses on the reaction mechanism of a bacterial ATP-citrate lyase.Ancient Regulatory Role of Lysine Acetylation in Central Metabolism.A novel ADP-forming succinyl-CoA synthetase in Thermococcus kodakaraensis structurally related to the archaeal nucleoside diphosphate-forming acetyl-CoA synthetases.
P2860

ADP-binding site of Escherichia coli succinyl-CoA synthetase revealed by x-ray crystallography

Item
http://www.wikidata.org/entity/Q27620927
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2000 nî lūn-bûn
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2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
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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
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name
ADP-binding site of Escherichi ...... ealed by x-ray crystallography
@ast
ADP-binding site of Escherichi ...... ealed by x-ray crystallography
@en
ADP-binding site of Escherichi ...... ealed by x-ray crystallography
@nl
type
label
ADP-binding site of Escherichi ...... ealed by x-ray crystallography
@ast
ADP-binding site of Escherichi ...... ealed by x-ray crystallography
@en
ADP-binding site of Escherichi ...... ealed by x-ray crystallography
@nl
prefLabel
ADP-binding site of Escherichi ...... ealed by x-ray crystallography
@ast
ADP-binding site of Escherichi ...... ealed by x-ray crystallography
@en
ADP-binding site of Escherichi ...... ealed by x-ray crystallography
@nl
P1433
P1476
P2093
P304
P31
P356
P407
P433
P478
P577
P698
P921
P356
P1433
P1476
ADP-binding site of Escherichi ...... ealed by x-ray crystallography
@en
P2093
P304
P31
P356
P407
P433
P478
P577
P698
P921