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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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Amos Bairoch

PROSITE documentation PDOC00979
Glucokinase regulatory protein family signature


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PURL: https://purl.expasy.org/prosite/documentation/PDOC00979

Description

The glucokinase regulatory protein (GCKR) [1] is a vertebrate protein that inhibits glucokinase by forming a complex with the enzyme, which plays a role in the control of blood glucose homeostasis. GCKR is a protein of about 70 Kd which is evolutionary related to bacterial N-acetylmuramic acid 6-phosphate etherases (MurNAc-6-P etherase, murQ) which are about half the size of GCKR and form active homodimers. MurNAc-6-P etherases catalyze the cleavage of the D-lactyl ether substituent of the bacterial cell wall sugar MurNAc and play a role in recycling of the cell wall [2]. The 3D structure of the Haemophilus influenzae HI0754/murQ protein (see <PDB:1NRI>) shows structural relationships with other sugar isomerase (SIS) domain proteins (see <PDOC51464>). In contrast to mono-SIS bacterial MurNAc-6-P etherase, mammalian GCKR is composed of two SIS domains.

As a signature pattern, we selected one of at least four well conserved regions found in those proteins.

Last update:

September 2009 / Text revised.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

GCKR, PS01272; Glucokinase regulatory protein family signature  (PATTERN)


References

1AuthorsVeiga-Da-Cunha M. Detheux M. Watelet N. Van Schaftingen E.
TitleCloning and expression of a Xenopus liver cDNA encoding a fructose-phosphate-insensitive regulatory protein of glucokinase.
SourceEur. J. Biochem. 225:43-51(1994).
PubMed ID7925465

2AuthorsJaeger T. Mayer C.
TitleN-acetylmuramic acid 6-phosphate lyases (MurNAc etherases): role in cell wall metabolism, distribution, structure, and mechanism.
SourceCell. Mol. Life Sci. 65:928-939(2008).
PubMed ID18049859
DOI10.1007/s00018-007-7399-



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