Allosteric coupling of two different functional active sites in monomeric Plasmodium falciparum glyoxalase I. (Q47839282)

6 February 2018

title

Allosteric coupling of two different functional active sites in monomeric Plasmodium falciparum glyoxalase I. (English)

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6 February 2018

main subject

Plasmodium falciparum

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6

Katja Becker

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6 February 2018

author name string

Marcel Deponte

1

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6 February 2018

Nicole Sturm

2

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Sarah Mittler

3

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6 February 2018

Max Harner

4

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Hildegard Mack

5

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language of work or name

English

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publication date

30 July 2007

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6 February 2018

Journal of Biological Chemistry

number of pages

12

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based on heuristic

inferred from page(s)

published in

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6 February 2018

volume

282

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issue

39

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6 February 2018

page(s)

28419-28430

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6 February 2018

Effect of pH and thiols on the kinetics of yeast glyoxalase I. Evaluation of the random pathway mechanism

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Reaction mechanism of glyoxalase I explored by an X-ray crystallographic analysis of the human enzyme in complex with a transition state analogue

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Yeast glyoxalase I is a monomeric enzyme with two active sites

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Characterization of the glyoxalases of the malarial parasite Plasmodium falciparum and comparison with their human counterparts

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ON THE NATURE OF ALLOSTERIC TRANSITIONS: A PLAUSIBLE MODEL

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Identification and phenotypic analysis of two glyoxalase II encoding genes from Saccharomyces cerevisiae, GLO2 and GLO4, and intracellular localization of the corresponding proteins

21 January 2018

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In situ analysis of methylglyoxal metabolism in Saccharomyces cerevisiae

21 January 2018

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21 January 2018

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Identifiers

DOI

10.1074/JBC.M703271200

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6 February 2018

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6 February 2018