Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway
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1.9 Å structure of the signal receiver domain of the putative response regulator NarL fromMycobacterium tuberculosisStructural Determinants of Substrate Recognition in the HAD Superfamily Member d - glycero - d - manno -Heptose-1,7-bisphosphate Phosphatase (GmhB),Structural and functional analysis of the phosphoryl transfer reaction mediated by the human small C-terminal domain phosphatase, Scp1Divergence of Structure and Function in the Haloacid Dehalogenase Enzyme Superfamily: Bacteroides thetaiotaomicron BT2127 Is an Inorganic PyrophosphataseStructural and Mechanistic Characterization of l -Histidinol Phosphate Phosphatase from the Polymerase and Histidinol Phosphatase Family of ProteinsStructural Basis for the Divergence of Substrate Specificity and Biological Function within HAD Phosphatases in Lipopolysaccharide and Sialic Acid BiosynthesisStructural Studies of Medicago truncatula Histidinol Phosphate Phosphatase from Inositol Monophosphatase Superfamily Reveal Details of Penultimate Step of Histidine Biosynthesis in PlantsSequence-based identification of inositol monophosphatase-like histidinol-phosphate phosphatases (HisN) in Corynebacterium glutamicum, Actinobacteria, and beyond.Divergence of biochemical function in the HAD superfamily: D-glycero-D-manno-heptose-1,7-bisphosphate phosphatase (GmhB).Histidine biosynthesis, its regulation and biotechnological application in Corynebacterium glutamicum.Biosynthesis of Histidine.HisB from Mycobacterium tuberculosis: cloning, overexpression in Mycobacterium smegmatis, purification, crystallization and preliminary X-ray crystallographic analysisPanoramic view of a superfamily of phosphatases through substrate profilingMolecular cloning, overexpression, purification, crystallization and preliminary X-ray diffraction studies of histidinol phosphate aminotransferase (HisC2) from Mycobacterium tuberculosisSubstrate ambiguous enzymes within the Escherichia coli proteome offer different evolutionary solutions to the same problem.Markers of fitness in a successful enzyme superfamily.Topological variation in the evolution of new reactions in functionally diverse enzyme superfamilies.A preliminary X-ray study of D,D-heptose-1,7-bisphosphate phosphatase from Burkholderia thailandensis E264.Cap-domain closure enables diverse substrate recognition by the C2-type haloacid dehalogenase-like sugar phosphatase Plasmodium falciparum HAD1Crystallization and preliminary X-ray crystallographic analysis of a novel histidinol-phosphate phosphatase from Thermococcus onnurineus NA1.Crystallization and preliminary X-ray diffraction analysis of Pseudomonas aeruginosa phosphorylcholine phosphatase.Novel monofunctional histidinol-phosphate phosphatase of the DDDD superfamily of phosphohydrolases
P2860
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P2860
Structural snapshots of Escherichia coli histidinol phosphate phosphatase along the reaction pathway
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2006 nî lūn-bûn
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2006 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
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2006 թվականի դեկտեմբերին հրատարակված գիտական հոդված
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2006年の論文
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2006年学术文章
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2006年学术文章
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2006年学术文章
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2006年学术文章
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Structural snapshots of Escher ...... ase along the reaction pathway
@ast
Structural snapshots of Escher ...... ase along the reaction pathway
@en
Structural snapshots of Escher ...... ase along the reaction pathway
@nl
type
label
Structural snapshots of Escher ...... ase along the reaction pathway
@ast
Structural snapshots of Escher ...... ase along the reaction pathway
@en
Structural snapshots of Escher ...... ase along the reaction pathway
@nl
prefLabel
Structural snapshots of Escher ...... ase along the reaction pathway
@ast
Structural snapshots of Escher ...... ase along the reaction pathway
@en
Structural snapshots of Escher ...... ase along the reaction pathway
@nl
P2093
P2860
P356
P1476
Structural snapshots of Escher ...... ase along the reaction pathway
@en
P2093
Ariane Proteau
Erumbi S Rangarajan
John Wagner
Ming-Ni Hung
P2860
P304
P356
10.1074/JBC.M604916200
P407
P577
2006-12-08T00:00:00Z