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Biochemistry (Moscow)

, Volume 80, Issue 13, pp 1672–1689 | Cite as

Sperm-Specific Glyceraldehyde-3-Phosphate Dehydrogenase–An Evolutionary Acquisition of Mammals

  • V. I. MuronetzEmail author
  • M. L. Kuravsky
  • K. V. Barinova
  • E. V. Schmalhausen
Review

Abstract

This review is focused on the mammalian sperm-specific glyceraldehyde-3-phosphate dehydrogenase (GAPDS). GAPDS plays the major role in the production of energy required for sperm cell movement and does not perform non-glycolytic functions that are characteristic of the somatic isoenzyme of glyceraldehyde-3-phosphate dehydrogenase. The GAPDS sequence is composed of 408 amino acid residues and includes an additional N-terminal region of 72 a.a. that binds the protein to the sperm tail cytoskeleton. GAPDS is present only in the sperm cells of mammals and lizards, possibly providing them with certain evolutionary advantages in reproduction. In this review, studies concerning the problems of GAPDS isolation, its catalytic properties, and its structural features are described in detail. GAPDS is much more stable compared to the somatic isoenzyme, perhaps due to the necessity of maintaining the enzyme function in the absence of protein expression. The site-directed mutagenesis approach revealed the two GAPDS-specific proline residues, as well as three salt bridges, which seem to be the basis of the increased stability of this protein. As distinct from the somatic isoenzyme, GAPDS exhibits positive cooperativity in binding of the coenzyme NAD+. The key role in transduction of structural changes induced by NAD+ is played by the salt bridge D311–H124. Disruption of this salt bridge cancels GAPDS cooperativity and twofold increases its enzymatic activity instead. The expression of GAPDS was detected in some melanoma cells as well. Its role in the development of certain pathologies, such as cancer and neurodegenerative diseases, is discussed.

Key words

glyceraldehyde-3-phosphate dehydrogenase sperm-specific glyceraldehyde-3-phosphate dehydrogenase GAPDH evolution of GAPDH stability of GAPDH sperm motility glycolysis melanoma cells oncomarker NAD-binding 

Abbreviations

GAPD

somatic glyceraldehyde-3-phosphate dehydrogenase

GAPDS

sperm-specific glyceraldehyde-3-phosphate dehydrogenase

GdnHCl

guanidine hydrochloride

Km

Michaelis constant.

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Copyright information

© Pleiades Publishing, Ltd. 2015

Authors and Affiliations

  • V. I. Muronetz
    • 1
    • 2
    Email author
  • M. L. Kuravsky
    • 1
  • K. V. Barinova
    • 1
    • 2
  • E. V. Schmalhausen
    • 1
  1. 1.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia
  2. 2.Faculty of Bioengineering and BioinformaticsLomonosov Moscow State UniversityMoscowRussia

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