Mutational analysis of the active site of indoleglycerol phosphate synthase from Escherichia coli.
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The crystal structure of indoleglycerol-phosphate synthase from Thermotoga maritima. Kinetic stabilization by salt bridgesStabilization of a (betaalpha)8-barrel protein by an engineered disulfide bridgeOccurrence of a putative ancient-like isomerase involved in histidine and tryptophan biosynthesisDirected evolution of new catalytic activity using the alpha/beta-barrel scaffold.Functional identification of the general acid and base in the dehydration step of indole-3-glycerol phosphate synthase catalysis.Molecular dynamics studies of ground state and intermediate of the hyperthermophilic indole-3-glycerol phosphate synthaseImidazole glycerol phosphate synthase from Thermotoga maritima. Quaternary structure, steady-state kinetics, and reaction mechanism of the bienzyme complex.
P2860
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P2860
Mutational analysis of the active site of indoleglycerol phosphate synthase from Escherichia coli.
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1998 nî lūn-bûn
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1998年の論文
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1998年学术文章
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name
Mutational analysis of the act ...... ynthase from Escherichia coli.
@ast
Mutational analysis of the act ...... ynthase from Escherichia coli.
@en
type
label
Mutational analysis of the act ...... ynthase from Escherichia coli.
@ast
Mutational analysis of the act ...... ynthase from Escherichia coli.
@en
prefLabel
Mutational analysis of the act ...... ynthase from Escherichia coli.
@ast
Mutational analysis of the act ...... ynthase from Escherichia coli.
@en
P2093
P2860
P356
P1433
P1476
Mutational analysis of the act ...... ynthase from Escherichia coli.
@en
P2093
Darimont B
Kirschner K
Szadkowski H
P2860
P304
P356
10.1002/PRO.5560070518
P577
1998-05-01T00:00:00Z