(Q34217801)

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A unified theory of enzyme kinetics based upon the systematic analysis of the variations of k(cat), K(M), and k(cat)/K(M) and the relevant DeltaG(0 not equal) values-possible implications in chemotherapy and biotechnology.

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11301037%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

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Europe PubMed Central

A unified theory of enzyme kinetics based upon the systematic analysis of the variations of k(cat), K(M), and k(cat)/K(M) and the relevant DeltaG(0 not equal) values-possible implications in chemotherapy and biotechnology (English)

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Europe PubMed Central

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11301037%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

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6 November 2019

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C Bauer

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6 November 2019

A M Osman

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6 November 2019

G Cercignani

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6 November 2019

N Gialluca

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6 November 2019

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1 May 2001

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6 November 2019

Biochemical Pharmacology

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6 November 2019

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6 November 2019

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6 November 2019

1049-1055

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6 November 2019

Energetics of proline racemase: racemization of unlabeled proline in the unsaturated, saturated, and oversaturated regimes

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Metal-substrate interactions facilitate the catalytic activity of the bacterial phosphotriesterase

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Asparagine-127 of xylanase A from Streptomyces lividans, a key residue in glycosyl hydrolases of superfamily 4/7: kinetic evidence for its involvement in stabilization of the catalytic intermediate

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7 January 2021

Regulation of trypsin activity by Cu2+ chelation of the substrate binding site.

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Multifunctional role of Tyr 108 in the catalytic mechanism of human glutathione transferase P1-1. Crystallographic and kinetic studies on the Y108F mutant enzyme

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Protein engineering of chimeric Serpins: an investigation into effects of the serpin scaffold and reactive centre loop length

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Specificity constants in the context of protein engineering of two-substrate enzymes

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A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework

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Impact of the lysine-188 and aspartic acid-189 inversion on activity of trypsin

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Getting a handhold on DNA: design of poly-zinc finger proteins with femtomolar dissociation constants.

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NAD(P)H (quinone acceptor) oxidoreductase (DT-diaphorase)-mediated two-electron reduction of anthraquinone-based antitumour agents and generation of hydroxyl radicals

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7 January 2021

Identifiers

10.1016/S0006-2952(01)00579-2

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Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11301037%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:11301037%20AND%20SRC:MED&resulttype=core&format=json

6 November 2019

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