The tyrosine-225 to phenylalanine mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both kcat and Km.
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Crystal structure of Escherichia coli cystathionine gamma-synthase at 1.5 A resolutionX-ray structure of MalY from Escherichia coli: a pyridoxal 5′-phosphate-dependent enzyme acting as a modulator in mal gene expressionCrystal Structure of a Homolog of Mammalian Serine Racemase from Schizosaccharomyces pombeStructural determinants for branched-chain aminotransferase isozyme-specific inhibition by the anticonvulsant drug gabapentinSulfur mobilization in cyanobacteria: the catalytic mechanism of L-cystine C-S lyase (C-DES) from synechocystis.Functional evolution of PLP-dependent enzymes based on active-site structural similaritiesPLP-dependent H(2)S biogenesis.Expression of apple 1-aminocyclopropane-1-carboxylate synthase in Escherichia coli: kinetic characterization of wild-type and active-site mutant forms.Chloroplastic aspartate aminotransferase from Arabidopsis thaliana: an examination of the relationship between the structure of the gene and the spatial structure of the protein.Histidine 282 in 5-aminolevulinate synthase affects substrate binding and catalysisQuantitative chimeric analysis of six specificity determinants that differentiate Escherichia coli aspartate from tyrosine aminotransferase.Active site model for gamma-aminobutyrate aminotransferase explains substrate specificity and inhibitor reactivities.Reactions of glutamate semialdehyde aminotransferase (glutamate-1-semialdehyde 2,1 aminomutase) with vinyl and acetylenic substrate analogues analysed by rapid scanning spectrophotometryThe mechanism of addition of pyridoxal 5'-phosphate to Escherichia coli apo-serine hydroxymethyltransferaseBrønsted analysis of aspartate aminotransferase via exogenous catalysis of reactions of an inactive mutant.Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.The structure of serine hydroxymethyltransferase as modeled by homology and validated by site-directed mutagenesis.Molecular and physiological analysis of Arabidopsis mutants defective in cytosolic or chloroplastic aspartate aminotransferase.Stereochemistry of the reactions of glutamate-1-semialdehyde aminomutase with 4,5-diaminovalerate.Identification of residues essential for the activity and substrate affinity of L-carnitine dehydrogenase.Human kynurenine aminotransferase II - reactivity with substrates and inhibitors
P2860
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P2860
The tyrosine-225 to phenylalanine mutation of Escherichia coli aspartate aminotransferase results in an alkaline transition in the spectrophotometric and kinetic pKa values and reduced values of both kcat and Km.
description
1991 nî lūn-bûn
@nan
1991年の論文
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1991年学术文章
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1991年学术文章
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1991年学术文章
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1991年学术文章
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1991年学术文章
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1991年学术文章
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1991年學術文章
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1991年學術文章
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name
The tyrosine-225 to phenylalan ...... ed values of both kcat and Km.
@en
The tyrosine-225 to phenylalan ...... ed values of both kcat and Km.
@nl
type
label
The tyrosine-225 to phenylalan ...... ed values of both kcat and Km.
@en
The tyrosine-225 to phenylalan ...... ed values of both kcat and Km.
@nl
prefLabel
The tyrosine-225 to phenylalan ...... ed values of both kcat and Km.
@en
The tyrosine-225 to phenylalan ...... ed values of both kcat and Km.
@nl
P2093
P356
P1433
P1476
The tyrosine-225 to phenylalan ...... ed values of both kcat and Km.
@en
P2093
Goldberg JM
Goodman HS
Swanson RV
P304
P356
10.1021/BI00215A041
P407
P577
1991-01-01T00:00:00Z