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PROSITE documentation PDOC00638

ADP-glucose pyrophosphorylase signatures


ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) [1,2] (EC catalyzes a very important step in the biosynthesis of α 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP.

ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. It is a homotetramer in bacteria while in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits.

There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. We selected three of these regions as signature patterns. The first two are N-terminal and have been proposed to be part of the allosteric and/or substrate-binding sites in the Escherichia coli enzyme (gene glgC). The third pattern corresponds to a conserved region in the central part of the enzymes.

Last update:

December 2004 / Patterns and text revised.

Technical section

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

ADP_GLC_PYROPHOSPH_1, PS00808; ADP-glucose pyrophosphorylase signature 1  (PATTERN)

ADP_GLC_PYROPHOSPH_2, PS00809; ADP-glucose pyrophosphorylase signature 2  (PATTERN)

ADP_GLC_PYROPHOSPH_3, PS00810; ADP-glucose pyrophosphorylase signature 3  (PATTERN)


1AuthorsNakata P.A. Greene T.W. Anderson J.M. Smith-White B.J. Okita T.W. Preiss J.
TitleComparison of the primary sequences of two potato tuber ADP-glucose pyrophosphorylase subunits.
SourcePlant Mol. Biol. 17:1089-1093(1991).
PubMed ID1657244

2AuthorsPreiss J. Ball K. Hutney J. Smith-White B.J. Li. L. Okitsa T.W.
SourcePure Appl. Chem. 63:535-544(1991).

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