Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis

Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis

Item
http://www.wikidata.org/entity/Q27642222
Crystal Structure of a Mammalian CTP: Phosphocholine Cytidylyltransferase Catalytic Domain Reveals Novel Active Site Residues within a Highly Conserved Nucleotidyltransferase FoldStructural Basis for Autoinhibition of CTP:Phosphocholine Cytidylyltransferase (CCT), the Regulatory Enzyme in Phosphatidylcholine Synthesis, by Its Membrane-binding Amphipathic HelixBiochemical characterization of Plasmodium falciparum CTP:phosphoethanolamine cytidylyltransferase shows that only one of the two cytidylyltransferase domains is activeCharacterization of the CDP-2-glycerol biosynthetic pathway in Streptococcus pneumoniaeCrystallization and preliminary X-ray analysis of CTP:phosphoethanolamine cytidylyltransferase (ECT) from Saccharomyces cerevisiae.Comparative kinetic analysis of glycerol 3-phosphate cytidylyltransferase from Enterococcus faecalis and Listeria monocytogenesThe ethanolamine branch of the Kennedy pathway is essential in the bloodstream form of Trypanosoma brucei.Glycerol Phosphate Cytidylyltransferase Stereospecificity Is Key to Understanding the Distinct Stereochemical Compositions of Glycerophosphoinositol in Bacteria and Archaea.Biosynthetic pathways of inositol and glycerol phosphodiesters used by the hyperthermophile Archaeoglobus fulgidus in stress adaptation.Contribution of each membrane binding domain of the CTP:phosphocholine cytidylyltransferase-alpha dimer to its activation, membrane binding, and membrane cross-bridging.Probing the active site of homoserine trans-succinylase.Two conserved histidine residues are critical to the function of the TagF-like family of enzymes.Crystal structure of D-glycero-Β-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei.An auto-inhibitory helix in CTP:phosphocholine cytidylyltransferase hi-jacks the catalytic residue and constrains a pliable, domain-bridging helix pair.Structural determinants of the catalytic mechanism of Plasmodium CCT, a key enzyme of malaria lipid biosynthesis
P2860

Glycerol-3-phosphate cytidylyltransferase. Structural changes induced by binding of CDP-glycerol and the role of lysine residues in catalysis

Item
http://www.wikidata.org/entity/Q27642222
description
2003 nî lūn-bûn
@nan
2003 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Glycerol-3-phosphate cytidylyl ...... f lysine residues in catalysis
@ast
Glycerol-3-phosphate cytidylyl ...... f lysine residues in catalysis
@en
Glycerol-3-phosphate cytidylyl ...... f lysine residues in catalysis
@nl
type
label
Glycerol-3-phosphate cytidylyl ...... f lysine residues in catalysis
@ast
Glycerol-3-phosphate cytidylyl ...... f lysine residues in catalysis
@en
Glycerol-3-phosphate cytidylyl ...... f lysine residues in catalysis
@nl
prefLabel
Glycerol-3-phosphate cytidylyl ...... f lysine residues in catalysis
@ast
Glycerol-3-phosphate cytidylyl ...... f lysine residues in catalysis
@en
Glycerol-3-phosphate cytidylyl ...... f lysine residues in catalysis
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P356
P1433
P1476
Glycerol-3-phosphate cytidylyl ...... f lysine residues in catalysis
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698