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MetaCyc Reaction: 2.7.7.9/2.7.7.64

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 2.7.7.9 , 2.7.7.64

Enzymes and Genes:

Arabidopsis thaliana col :
Bacillus subtilis : UTP-glucose-1-phosphate uridylyltransferase Inferred from experiment : gtaB
Cucumis melo :
Escherichia coli K-12 substr. MG1655 : UTP--glucose-1-phosphate uridylyltransferase Inferred from experiment : galU
Haloferax volcanii : UTP--glucose-1-phosphate uridylyltransferase Inferred from experiment : aglF
Homo sapiens : UDP-glucose pyrophosphorylase Inferred from experiment : UGP2
Leishmania major : UDP-sugar pyrophosphorylase Inferred from experiment : USP
Mus musculus : UDP-glucose pyrophosphorylase 2 Inferred by curator Inferred from experiment : Ugp2
Mycoplasma pneumoniae M129 : UDP-glucose pyrophosphorylase Inferred from experiment : galU
Pisum sativum : UDP-D-glucose pyrophosphorylase Inferred from experiment : USP
Saccharomyces cerevisiae : UDP-glucose pyrophosphorylase Inferred from experiment : UGP1

In Pathway: chitin biosynthesis , stachyose degradation , sucrose biosynthesis II , UDP-glucose biosynthesis , sucrose degradation II (sucrose synthase)

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.

Mass balance status: Balanced.

Enzyme Commission Primary Name for 2.7.7.9: UTP—glucose-1-phosphate uridylyltransferase

Enzyme Commission Synonyms for 2.7.7.9: UDP glucose pyrophosphorylase, glucose-1-phosphate uridylyltransferase, UDPG phosphorylase, UDPG pyrophosphorylase, uridine 5'-diphosphoglucose pyrophosphorylase, uridine diphosphoglucose pyrophosphorylase, uridine diphosphate-D-glucose pyrophosphorylase, uridine-diphosphate glucose pyrophosphorylase

Enzyme Commission Primary Name for 2.7.7.64: UTP-monosaccharide-1-phosphate uridylyltransferase

Enzyme Commission Synonyms for 2.7.7.64: UDP-sugar pyrophosphorylase, PsUSP

Standard Gibbs Free Energy (ΔrG in kcal/mol): -103.30347 Inferred by computational analysis [Latendresse13]

Enzyme Commission Summary for 2.7.7.64:
The reaction can occur in either direction and it has been postulated that MgUTP and Mg-diphosphate are the actual substrates. Catalyzes the formation of UDP-Glc, UDP-Gal, UDP-GlcA, UDP-L-Ara and UDP-Xyl, showing broad substrate specificity toward monosaccharide 1-phosphates. Mannose 1-phosphate, L-fucose 1-phosphate and glucose 6-phosphate are not substrates and UTP cannot be replaced by other nucleotide triphosphates.

Citations: [Dai06, LobelleRich83, Kamogawa65, KALCKAR, SMITH55, Turnquist74, Rudick74, Kotake04]

Gene-Reaction Schematic: ?

Gene-Reaction Schematic

Instance reactions of [UTP + a sugar 1-phosphate + H+ ↔ a UDP-sugar + diphosphate] (2.7.7.64):
i1: α-D-galactose 1-phosphate + UTP + H+ ↔ UDP-α-D-galactose + diphosphate (2.7.7.10/2.7.7.64)

i2: α-D-glucopyranose 1-phosphate + UTP + H+ ↔ UDP-α-D-glucose + diphosphate (2.7.7.9/2.7.7.64)
i3: UTP + N-acetyl-α-D-galactosamine 1-phosphate + H+ = UDP-N-acetyl-α-D-galactosamine + diphosphate (2.7.7.83)

i4: N-acetyl-α-D-glucosamine 1-phosphate + UTP + H+ → UDP-N-acetyl-α-D-glucosamine + diphosphate (2.7.7.23)

i5: α-D-xylose 1-phosphate + UTP + H+ ↔ UDP-α-D-xylose + diphosphate (2.7.7.11)

Unification Links: KEGG:R00289 , PIR:A40650 , PIR:A41382 , PIR:A56146 , PIR:A64250 , PIR:A64970 , PIR:A75096 , PIR:D49349 , PIR:D69184 , PIR:D70601 , PIR:E64466 , PIR:E71913 , PIR:F59102 , PIR:F64600 , PIR:F81300 , PIR:G64095 , PIR:G70125 , PIR:H70446 , PIR:JC2265 , PIR:JC4785 , PIR:JC4985 , PIR:JX0277 , PIR:S15298 , PIR:S30007 , PIR:S31431 , PIR:S35692 , PIR:S41533 , PIR:S62599 , PIR:S73501 , PIR:S78541 , PIR:T42521 , PIR:T44841 , PIR:T45453 , PIR:XNDOU , PIR:XNPOU , Rhea:19889 , UniProt:O05576 , UniProt:O25363 , UniProt:O26731 , UniProt:O51225 , UniProt:O67602 , UniProt:P08800 , UniProt:P0AAB6 , UniProt:P0AEP3 , UniProt:P19595 , UniProt:P27897 , UniProt:P32861 , UniProt:P33696 , UniProt:P37776 , UniProt:P44878 , UniProt:P47691 , UniProt:P74969 , UniProt:P75124 , UniProt:P78811 , UniProt:Q9PMD3 , UniProt:Q9RMC3 , UniProt:Q9UZI7 , UniProt:Q9X364 , UniProt:Q9Z5G1 , UniProt:Q9ZLI8 , UniProt:Q05852 , UniProt:Q07130 , UniProt:Q07131 , UniProt:Q43772 , UniProt:Q46768 , UniProt:Q48447 , UniProt:Q58730

Relationship Links: BRENDA:EC:2.7.7.9 , BRENDA:EC:2.7.7.64 , ENZYME:EC:2.7.7.9 , ENZYME:EC:2.7.7.64 , IUBMB-ExplorEnz:EC:2.7.7.9 , IUBMB-ExplorEnz:EC:2.7.7.64 , UniProt:RELATED-TO:O05576 , UniProt:RELATED-TO:O25363 , UniProt:RELATED-TO:O26731 , UniProt:RELATED-TO:O51225 , UniProt:RELATED-TO:O67602 , UniProt:RELATED-TO:P08800 , UniProt:RELATED-TO:P0AAB6 , UniProt:RELATED-TO:P0AEP3 , UniProt:RELATED-TO:P19595 , UniProt:RELATED-TO:P27897 , UniProt:RELATED-TO:P32861 , UniProt:RELATED-TO:P33696 , UniProt:RELATED-TO:P37776 , UniProt:RELATED-TO:P44878 , UniProt:RELATED-TO:P47691 , UniProt:RELATED-TO:P74969 , UniProt:RELATED-TO:P75124 , UniProt:RELATED-TO:P78811 , UniProt:RELATED-TO:Q9PMD3 , UniProt:RELATED-TO:Q9RMC3 , UniProt:RELATED-TO:Q9UZI7 , UniProt:RELATED-TO:Q9X364 , UniProt:RELATED-TO:Q9Z5G1 , UniProt:RELATED-TO:Q9ZLI8 , UniProt:RELATED-TO:Q05852 , UniProt:RELATED-TO:Q07130 , UniProt:RELATED-TO:Q07131 , UniProt:RELATED-TO:Q43772 , UniProt:RELATED-TO:Q46768 , UniProt:RELATED-TO:Q48447 , UniProt:RELATED-TO:Q58730

Credits:
Created 18-Jun-2010 by Pujar A , Boyce Thompson Institute


References

Dai06: Dai N, Petreikov M, Portnoy V, Katzir N, Pharr DM, Schaffer AA (2006). "Cloning and expression analysis of a UDP-galactose/glucose pyrophosphorylase from melon fruit provides evidence for the major metabolic pathway of galactose metabolism in raffinose oligosaccharide metabolizing plants." Plant Physiol 142(1);294-304. PMID: 16829585

KALCKAR: KALCKAR HM "The role of phosphoglycosyl compounds in the biosynthesis of nucleosides and nucleotides." Biochim Biophys Acta 12(1-2);250-64. PMID: 13115434

Kamogawa65: Kamogawa A, Kurahashi K (1965). "Purification and properties of uridinediphosphate glucose pyrophosphorylase from Escherichia coli K12." J Biochem 57(6);758-65. PMID: 4284510

Kotake04: Kotake T, Yamaguchi D, Ohzono H, Hojo S, Kaneko S, Ishida HK, Tsumuraya Y (2004). "UDP-sugar pyrophosphorylase with broad substrate specificity toward various monosaccharide 1-phosphates from pea sprouts." J Biol Chem 279(44);45728-36. PMID: 15326166

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

LobelleRich83: Lobelle-Rich PA, Reeves RE (1983). "Separation and characterization of two UTP-utilizing hexose phosphate uridylyltransferases from Entamoeba histolytica." Mol Biochem Parasitol 7(2);173-82. PMID: 6304512

Rudick74: Rudick VL, Weisman RA (1974). "Uridine diphosphate glucose pyrophosphorylase of Acanthamoeba castellanii. Purification, kinetic, and developmental studies." J Biol Chem 249(24);7832-40. PMID: 4430676

SMITH55: SMITH EE, MILLS GT (1955). "The uridyl transferase of mammary gland." Biochim Biophys Acta 18(1);152. PMID: 13260264

Turnquist74: Turnquist RL, Gillett TA, Hansen RG (1974). "Uridine diphosphate glucose pyrophosphorylase. Crystallization and properties of the enzyme from rabbit liver and species comparisons." J Biol Chem 249(23);7695-700. PMID: 4436332


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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 19.0 on Thu Jul 30, 2015, biocyc13.