Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.
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Janus: 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 aminotransferasesRedesign of choline acetyltransferase specificity by protein engineering.Investigating and Engineering Enzymes by Genetic Selection.Redesign of substrate-selectivity determining modules of glutathione transferase A1-1 installs high catalytic efficiency with toxic alkenal products of lipid peroxidation.Evolutionary recruitment of biochemically specialized subdivisions of Family I within the protein superfamily of aminotransferases.Directed evolution of an aspartate aminotransferase with new substrate specificitiesA streptavidin mutant with altered ligand-binding specificityAspartate aminotransferase: an old dog teaches new tricks.Recombinant expression of twelve evolutionarily diverse subfamily Ialpha aminotransferasesQuantitative chimeric analysis of six specificity determinants that differentiate Escherichia coli aspartate from tyrosine aminotransferase.Directed evolution relieves product inhibition and confers in vivo function to a rationally designed tyrosine aminotransferase.Defective regulation of autophagy upon leucine deprivation reveals a targetable liability of human melanoma cells in vitro and in vivo.Site-saturation mutagenesis is more efficient than DNA shuffling for the directed evolution of beta-fucosidase from beta-galactosidase.Mechanistic and Evolutionary Insights from Comparative Enzymology of Phosphomonoesterases and Phosphodiesterases across the Alkaline Phosphatase SuperfamilyPLP and GABA trigger GabR-mediated transcription regulation in Bacillus subtilis via external aldimine formationEngineering homooligomeric proteins to detect weak intersite allosteric communication: aminotransferases, a case study.The use of natural and unnatural amino acid substrates to define the substrate specificity differences of Escherichia coli aspartate and tyrosine aminotransferases.Molecular function prediction for a family exhibiting evolutionary tendencies toward substrate specificity swapping: recurrence of tyrosine aminotransferase activity in the Iα subfamily.Use of indirect site-directed mutagenesis to alter the substrate specificity of methylamine dehydrogenase.Phenylalanine catabolism in Archaeoglobus fulgidus VC-16.Thermodynamics and molecular simulation analysis of hydrophobic substrate recognition by aminotransferases.Selective Targeting by a Mechanism-Based Inactivator against Pyridoxal 5'-Phosphate-Dependent Enzymes: Mechanisms of Inactivation and Alternative Turnover.Hydrolysis of phosphodiesters through transformation of the bacterial phosphotriesterase.Tailoring the specificity of the type C feruloyl esterase FoFaeC from Fusarium oxysporum towards methyl sinapate by rational redesign based on small molecule docking simulations.
P2860
Q27676283-8D8A37CF-D727-431A-A3B3-186D3AD08BBEQ27766665-9E6B812F-6B5C-45BB-9433-8D9942A9BFDDQ28364597-109596F2-DF15-400E-A21D-C385A63F15D7Q28583918-2D6AE219-157F-4DEC-BAE5-3D0516FDB6D3Q30431401-CA719549-DF05-4A98-AEF0-11F42982C037Q30731663-F560FA8A-FF5D-48FD-A59B-BA461F3A6F5AQ35206059-C53BA4F4-2483-481D-BCDE-65D879430419Q35605169-D72D9EA2-D6EA-4BA2-975E-2950D8663D78Q36089937-5A093F7A-2CE2-4CB1-98F6-0C4C7992BFECQ36792599-85AEF7F3-0263-436A-BA67-C2479582161FQ37624340-30B22D52-C9C4-4EEE-9460-BD67099DBC58Q37858839-D5D64D00-26AB-4BD4-93CB-3A986584D147Q38270604-59C5D5DD-C272-4B12-BE06-6DE388E39583Q38344979-A0578804-2517-43E2-A4FA-C18D4DDC501EQ39541632-B9DAB0C5-161E-499D-8885-90060A1CAA48Q41605240-02587171-F4F5-4264-A0FC-83A8DFAF951FQ41676786-A62CA0C3-9548-4DF7-8633-C696BD607589Q42140394-1490A27D-E7C1-4CAF-B3E9-85A8D007BBAFQ42583709-FDEE1ADE-32BB-483E-B5D9-F70222C6FC02Q42844917-D952AD95-0D5C-4513-A4FE-A036076BA86CQ42914294-118148A4-BF2D-4C86-A377-A65BC6E3B324Q43815811-42E7984F-BC1E-4E1A-845E-47AD725E986AQ46020626-0433EE03-3935-48BE-8812-208D2E2A79B2Q47859631-1EB1BE1B-D73B-4A7C-807A-5565B3FA9BA2Q47941755-B0B7B6A0-935C-48D9-85AD-2BD07DAEE281Q52564371-D800103E-D39F-41B0-9430-986A2838AD82Q55083118-19225BD4-3A9F-457C-82CF-7F60613C9B59
P2860
Redesign of the substrate specificity of Escherichia coli aspartate aminotransferase to that of Escherichia coli tyrosine aminotransferase by homology modeling and site-directed mutagenesis.
description
1995 nî lūn-bûn
@nan
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
1995年论文
@zh
1995年论文
@zh-cn
name
Redesign of the substrate spec ...... and site-directed mutagenesis.
@en
Redesign of the substrate spec ...... and site-directed mutagenesis.
@nl
type
label
Redesign of the substrate spec ...... and site-directed mutagenesis.
@en
Redesign of the substrate spec ...... and site-directed mutagenesis.
@nl
prefLabel
Redesign of the substrate spec ...... and site-directed mutagenesis.
@en
Redesign of the substrate spec ...... and site-directed mutagenesis.
@nl
P2860
P356
P1433
P1476
Redesign of the substrate spec ...... and site-directed mutagenesis.
@en
P2093
J F Kirsch
J J Onuffer
P2860
P304
P356
10.1002/PRO.5560040910
P577
1995-09-01T00:00:00Z