Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme (scientific article published on April 1985)

Dihydroxyacetone phosphate. Its structure and reactivity with -glycerophosphate dehydrogenase, aldolase and triose phosphate isomerase and some possible metabolic implications

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A rapid boiling method for the preparation of bacterial plasmids

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Influence of pH on the interaction of inhibitors with triosephosphate isomerase and determination of the pKa of the active-site carboxyl group

Q30104772

Prolonged incubation in calcium chloride improves the competence of Escherichia coli cells

Q34192132

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Deletion mapping of the polA-metB region of the Escherichia coli chromosome

Q36337778

Chicken triosephosphate isomerase complements an Escherichia coli deficiency

Q36488403

6 Statistical analysis of enzyme kinetic data

Q36541244

Nucleotide sequence of the triose phosphate isomerase gene of Saccharomyces cerevisiae.

Q36628143

Metabolism of methylglyoxal in microorganisms

Q40078802

Solid phase synthesis of polynucleotides. VI. Further studies on polystyrene copolymers for the solid support

Q40463890

Rapid and efficient cosmid cloning

Q40499096

Oligonucleotide directed mutagenesis of the human beta-globin gene: a general method for producing specific point mutations in cloned DNA.

Q40499415

The active centre of rabbit muscle triose phosphate isomerase. The site that is labelled by glycidol phosphate

Q41894027

The active chemical state of D-glyceraldehyde 3-phosphate in its reactions with D-glyceraldehyde 3-phosphate dehydrogenase, aldolase and triose phosphate isomerase

Q42140712

The existence of an electrophilic component in the reaction catalysed by triose phosphate isomerase.

Q42151063

Specificity and kinetics of triose phosphate isomerase from chicken muscle

Q42918877

Identification of Site in Triose Phosphate Isomerase Labelled by Glycidol Phosphate

Q43630604

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Q43646870

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Probing the catalytic mechanism of yeast triose phosphate isomerase by site-specific mutagenesis

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Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy

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Uniquely Labelled Active Site Sequence in Chicken Muscle Triose Phosphate Isomerase

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Isolation and characterization of an active-site peptide from triose phosphate isomerase

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Site-specific mutagenesis of aspartate transcarbamoylase. Replacement of tyrosine 165 in the catalytic chain by serine reduces enzymatic activity

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GLYCOLYTIC CONTROL MECHANISMS. I. INHIBITION OF GLYCOLYSIS BY ACETATE AND PYRUVATE IN THE ISOLATED, PERFUSED RAT HEART

Q78405503

P433

issue

P407

language of work or name

English

Q1860

P304

page(s)

2272-2276

P577

publication date

1985-04-01

P1433

published in

Proceedings of the National Academy of Sciences of the United States of America

Q1146531

P1476

title

Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme

P478

volume

Reverse relations

cites work (P2860)

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Q43213976	Cross-species analysis of the glycolytic pathway by comparison of molecular interaction fields
Q42844591	Crystal structure of recombinant triosephosphate isomerase from Bacillus stearothermophilus. An analysis of potential thermostability factors in six isomerases with known three-dimensional structures points to the importance of hydrophobic interacti
Q33954766	Effects of amino acid substitutions at the active site in Escherichia coli beta-galactosidase
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Q30968138	Identification of residues critical for catalysis in a class C beta-lactamase by combinatorial scanning mutagenesis
Q37402992	Importance of a hydrophobic residue in binding and catalysis by dihydrofolate reductase
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Q24559878	Searching sequence space by definably random mutagenesis: improving the catalytic potency of an enzyme
Q68926998	Site-directed mutagenesis
Q35594207	Site-saturation studies of beta-lactamase: production and characterization of mutant beta-lactamases with all possible amino acid substitutions at residue 71
Q37068901	Structure-Function Studies of Hydrophobic Residues That Clamp a Basic Glutamate Side Chain during Catalysis by Triosephosphate Isomerase
Q57961331	The Mechanistic Pathway of a Mutant Triosephosphate Isomerase
Q33909033	Triosephosphate isomerase: 15N and 13C chemical shift assignments and conformational change upon ligand binding by magic-angle spinning solid-state NMR spectroscopy
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Q30365015	qPIPSA: relating enzymatic kinetic parameters and interaction fields.

P819	ADS bibcode	1985PNAS...82.2272S
P356	DOI	10.1073/PNAS.82.8.2272
P932	PMC publication ID	397539
P698	PubMed publication ID	3887397
P5875	ResearchGate publication ID	19275337