Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase
about
Crystal structures of Mycobacterium tuberculosis HspAT and ArAT reveal structural basis of their distinct substrate specificities.Crystal structure of trypanosoma cruzi tyrosine aminotransferase: Substrate specificity is influenced by cofactor binding modeFree energy requirement for domain movement of an enzymeThe trimer-of-hairpins motif in membrane fusion: Visna virusJanus: Prediction and Ranking of Mutations Required for Functional Interconversion of EnzymesRedesigning the substrate specificity of an enzyme by cumulative effects of the mutations of non-active site residuesA general method for the quantitative analysis of functional chimeras: applications from site-directed mutagenesis and macromolecular associationInvolvement of conserved asparagine and arginine residues from the N-terminal region in the catalytic mechanism of rat liver and Trypanosoma cruzi tyrosine aminotransferasesFunctional evolution of PLP-dependent enzymes based on active-site structural similaritiesEvolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases.Active-Site Engineering of ω-Transaminase for Production of Unnatural Amino Acids Carrying a Side Chain Bulkier than an Ethyl Substituent.Directed evolution of an aspartate aminotransferase with new substrate specificitiesFeatures and technical applications of ω-transaminases.Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase.Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase SuperfamilyThe use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases.Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.Structural studies of the catalytic reaction pathway of a hyperthermophilic histidinol-phosphate aminotransferase.Molecular determinants for substrate selectivity of ω-transaminases.Thermodynamics and molecular simulation analysis of hydrophobic substrate recognition by aminotransferases.
P2860
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P2860
Alternating arginine-modulated substrate specificity in an engineered tyrosine aminotransferase
description
1995 nî lūn-bûn
@nan
1995 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Alternating arginine-modulated ...... ered tyrosine aminotransferase
@ast
Alternating arginine-modulated ...... ered tyrosine aminotransferase
@en
Alternating arginine-modulated ...... ered tyrosine aminotransferase
@nl
type
label
Alternating arginine-modulated ...... ered tyrosine aminotransferase
@ast
Alternating arginine-modulated ...... ered tyrosine aminotransferase
@en
Alternating arginine-modulated ...... ered tyrosine aminotransferase
@nl
prefLabel
Alternating arginine-modulated ...... ered tyrosine aminotransferase
@ast
Alternating arginine-modulated ...... ered tyrosine aminotransferase
@en
Alternating arginine-modulated ...... ered tyrosine aminotransferase
@nl
P2093
P2860
P356
P1476
Alternating arginine-modulated ...... ered tyrosine aminotransferase
@en
P2093
J F Kirsch
J J Onuffer
J N Jansonius
V N Malashkevich
P2860
P304
P356
10.1038/NSB0795-548
P577
1995-07-01T00:00:00Z