Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase.
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Crystal structures of Mycobacterium tuberculosis HspAT and ArAT reveal structural basis of their distinct substrate specificities.Structural Analysis and Mutant Growth Properties Reveal Distinctive Enzymatic and Cellular Roles for the Three Major L-Alanine Transaminases of Escherichia coliIdentification of novel bacterial histidine biosynthesis inhibitors using docking, ensemble rescoring, and whole-cell assaysBiosynthesis of Histidine.Global Dynamic Proteome Study of a Pellicle-forming Acinetobacter baumannii Strain.Repurposed HisC Aminotransferases Complete the Biosynthesis of Some Methanobactins.
P2860
Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase.
description
2004 nî lūn-bûn
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name
Structural studies of the cata ...... ol-phosphate aminotransferase.
@en
Structural studies of the cata ...... ol-phosphate aminotransferase.
@nl
type
label
Structural studies of the cata ...... ol-phosphate aminotransferase.
@en
Structural studies of the cata ...... ol-phosphate aminotransferase.
@nl
prefLabel
Structural studies of the cata ...... ol-phosphate aminotransferase.
@en
Structural studies of the cata ...... ol-phosphate aminotransferase.
@nl
P2093
P2860
P356
P1476
Structural studies of the cata ...... ol-phosphate aminotransferase.
@en
P2093
Erika Sandmeier
Frank Lehmann
Heinz Gehring
M Cristina Vega
Philipp Christen
P2860
P304
21478-21488
P356
10.1074/JBC.M400291200
P407
P577
2004-03-08T00:00:00Z