Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase
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Conformational change in aspartate aminotransferase on substrate binding induces strain in the catalytic group and enhances catalysisCrystal structures of threonine synthase from Thermus thermophilus HB8: conformational change, substrate recognition, and mechanismA Structural Study of GDP-4-Keto-6-Deoxy- d -Mannose-3-Dehydratase: Caught in the Act of Geminal Diamine Formation † , ‡Structural Analysis and Mutant Growth Properties Reveal Distinctive Enzymatic and Cellular Roles for the Three Major L-Alanine Transaminases of Escherichia coliCrystal structure and enzymatic properties of a broad substrate-specificity psychrophilic aminotransferase from the Antarctic soil bacterium Psychrobacter sp. B6PLP-dependent H(2)S biogenesis.Laue and monochromatic diffraction studies on catalysis in phosphorylase b crystals.Tyrosine phenol-lyase and tryptophan indole-lyase encapsulated in wet nanoporous silica gels: Selective stabilization of tertiary conformationsAspartate aminotransferase: an old dog teaches new tricks.Ornithine Aminotransferase, an Important Glutamate-Metabolizing Enzyme at the Crossroads of Multiple Metabolic Pathways.Flexibility, diversity, and cooperativity: pillars of enzyme catalysis.Ornithine aminotransferase versus GABA aminotransferase: implications for the design of new anticancer drugs.The role of the conserved Lys68*:Glu265 intersubunit salt bridge in aspartate aminotransferase kinetics: multiple forced covariant amino acid substitutions in natural variants.Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase.The structure of GDP-4-keto-6-deoxy-D-mannose-3-dehydratase: a unique coenzyme B6-dependent enzyme.The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases.Noncovalent binding of a reaction intermediate by a designed helix-loop-helix motif-implications for catalyst design.Active-site Arg --> Lys substitutions alter reaction and substrate specificity of aspartate aminotransferase.Quantum Mechanics/Molecular Mechanics Studies on the Mechanism of Action of Cofactor Pyridoxal 5′-Phosphate in Ornithine 4,5-Aminomutase
P2860
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P2860
Crystal structures of true enzymatic reaction intermediates: aspartate and glutamate ketimines in aspartate aminotransferase
description
1993 nî lūn-bûn
@nan
1993 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1993 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1993年の論文
@ja
1993年論文
@yue
1993年論文
@zh-hant
1993年論文
@zh-hk
1993年論文
@zh-mo
1993年論文
@zh-tw
1993年论文
@wuu
name
Crystal structures of true enz ...... in aspartate aminotransferase
@ast
Crystal structures of true enz ...... in aspartate aminotransferase
@en
Crystal structures of true enz ...... in aspartate aminotransferase
@nl
type
label
Crystal structures of true enz ...... in aspartate aminotransferase
@ast
Crystal structures of true enz ...... in aspartate aminotransferase
@en
Crystal structures of true enz ...... in aspartate aminotransferase
@nl
prefLabel
Crystal structures of true enz ...... in aspartate aminotransferase
@ast
Crystal structures of true enz ...... in aspartate aminotransferase
@en
Crystal structures of true enz ...... in aspartate aminotransferase
@nl
P2093
P356
P1433
P1476
Crystal structures of true enz ...... in aspartate aminotransferase
@en
P2093
J N Jansonius
V N Malashkevich
P304
P356
10.1021/BI00212A010
P407
P577
1993-12-14T00:00:00Z