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| {{enzyme
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| | Name = glucose-1-phosphate adenylyltransferase
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| | EC_number = 2.7.7.27
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| | CAS_number = 9027-71-8
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| | IUBMB_EC_number = 2/7/7/27
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| | GO_code = 0008878
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| In [[enzymology]], a '''glucose-1-phosphate adenylyltransferase''' ({{EC number|2.7.7.27}}) is an [[enzyme]] that [[catalysis|catalyzes]] the [[chemical reaction]]
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| :ATP + alpha-D-glucose 1-phosphate <math>\rightleftharpoons</math> diphosphate + ADP-glucose
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| Thus, the two [[substrate (biochemistry)|substrates]] of this enzyme are [[adenosine triphosphate|ATP]] and [[alpha-D-glucose 1-phosphate]], whereas its two [[product (chemistry)|products]] are [[diphosphate]] and [[ADP-glucose]].
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| This enzyme belongs to the family of [[transferase]]s, specifically those transferring phosphorus-containing [[nucleotide]] groups ([[nucleotidyltransferase]]s). The systematic name of this enzyme class is '''ATP:alpha-D-glucose-1-phosphate adenylyltransferase'''. Other names in common use include '''ADP glucose pyrophosphorylase''', '''glucose 1-phosphate adenylyltransferase''', '''adenosine diphosphate glucose pyrophosphorylase''', '''adenosine diphosphoglucose pyrophosphorylase''', '''ADP-glucose pyrophosphorylase''', '''ADP-glucose synthase''', '''ADP-glucose synthetase''', '''ADPG pyrophosphorylase''', '''ADP:alpha-D-glucose-1-phosphate adenylyltransferase''' and '''AGPase'''. This enzyme participates in [[starch and sucrose metabolism]].
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| ==Structural studies==
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| As of late 2007, 3 [[tertiary structure|structures]] have been solved for this class of enzymes, with [[Protein Data Bank|PDB]] accession codes {{PDB link|1YP2}}, {{PDB link|1YP3}}, and {{PDB link|1YP4}}.
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| ==References==
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| {{reflist|1}}
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| * {{cite journal | author = Ghosh HP, Preiss J | date = 1966 | title = Adenosine diphosphate glucose pyrophosphorylase. A regulatory enzyme in the biosynthesis of starch in spinach leaf chloroplasts | journal = J. Biol. Chem. | volume = 241 | pages = 4491–504 | pmid = 5922972 | issue = 19 }}
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| * {{cite journal | author = Shen L and Preiss J | date = 1965 | title = Biosynthesis of bacterial glycogen. I. Purification and properties of the adenosine diphosphoglucose pyrophosphorylase of Arthrobacter species NRRL B1973 | journal = J. Biol. Chem. | volume = 240 | pages = 2334–2340 }}
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| {{enzyme-stub}}
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| [[Category:EC 2.7.7]]
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| [[Category:Enzymes of known structure]]
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