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Literature summary extracted from

  • McCorvie, T.J.; Timson, D.J.
    The structural and molecular biology of type I galactosemia: enzymology of galactose 1-phosphate uridylyltransferase (2011), IUBMB Life, 63, 694-700.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.7.7.12 drug development the enzyme might be a target for inhibitor design in galactosemia treatment Homo sapiens

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.7.12 crystal structure determination and analysis Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.12 ADP
-
 Homo sapiens
2.7.7.12 ADP-glucose
-
 Homo sapiens
2.7.7.12 alpha-D-galactose 1-phosphate competitive substrate inhibition in the forward reaction Escherichia coli
2.7.7.12 alpha-D-galactose 1-phosphate competitive substrate inhibition in the forward reaction Homo sapiens
2.7.7.12 ATP
-
 Homo sapiens
2.7.7.12 CDP-glucose
-
 Homo sapiens
2.7.7.12 diethyl dicarbonate inactivates the enzyme, reversable by hydroxylamine Escherichia coli
2.7.7.12 GDP-glucose
-
 Homo sapiens
2.7.7.12 TDP-glucose
-
 Homo sapiens
2.7.7.12 UDP
-
 Homo sapiens
2.7.7.12 UDP-galactose the product of the forward reaction is a competitive inhibitor with respect to UDP-glucose and a mixed inhibitor with respect to galactose 1-phosphate Escherichia coli
2.7.7.12 UDP-galactose the product of the forward reaction is a competitive inhibitor with respect to UDP-glucose and a mixed inhibitor with respect to galactose 1-phosphate Homo sapiens
2.7.7.12 UDP-glucuronic acid
-
 Homo sapiens
2.7.7.12 UDP-mannose
-
 Homo sapiens
2.7.7.12 UDP-xylose
-
 Homo sapiens
2.7.7.12 UMP
-
 Homo sapiens
2.7.7.12 Uracil
-
 Homo sapiens
2.7.7.12 uridine
-
 Homo sapiens
2.7.7.12 UTP
-
 Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.7.12 Fe2+ the enzyme homodimer contains one zinc (II) and one iron (II) ion per subunit, pyramidial iron-binding site, structure, overview Escherichia coli
2.7.7.12 Zn2+ the enzyme homodimer contains one zinc (II) and one iron (II) ion per subunit, tetrahedral zinc binding site, structure, overview Escherichia coli
2.7.7.12 Zn2+ the zinc co-orientating residues are not conserved and therefore, it may only bind one metal ion per monomer Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.7.7.12 UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate Escherichia coli
-
 alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
 r
2.7.7.12 UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate Homo sapiens
-
 alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.12 Escherichia coli
-
-
-
2.7.7.12 Homo sapiens
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.7.12 UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose ping-pong catalytic mechanism, a UMP group is transferred from UDP-glucose to His186 in the active site of the enzyme, overview Homo sapiens
a
2.7.7.12 UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate = alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose ping-pong catalytic mechanism, overview. A UMP group is transferred from UDP-glucose to His166 in the active site of the enzyme Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.12 additional information the enzyme has a strict requirement for UDP-glucose or UDP-galactose as substrates, while GDP-glucose, ADP-glucose, TDP-glucose, CDP-glucose, UDPxylose, and UDP-mannose are all unable to support activity Escherichia coli ?
-
 ?
2.7.7.12 additional information the enzyme has a strict requirement for UDP-glucose or UDP-galactose as substrates, while GDP-glucose, ADP-glucose, TDP-glucose, CDP-glucose, UDPxylose, and UDP-mannose are all unable to support activity Homo sapiens ?
-
 ?
2.7.7.12 UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
-
 Escherichia coli alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
 r
2.7.7.12 UDP-alpha-D-glucose + alpha-D-galactose 1-phosphate
-
 Homo sapiens alpha-D-glucose 1-phosphate + UDP-alpha-D-galactose
-
 r

Subunits

EC Number Subunits Comment Organism
2.7.7.12 homodimer
-
 Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.7.7.12 galactose 1-phosphate uridylyltransferase
-
 Escherichia coli
2.7.7.12 galactose 1-phosphate uridylyltransferase
-
 Homo sapiens
2.7.7.12 GALT
-
 Escherichia coli
2.7.7.12 GALT
-
 Homo sapiens

General Information

EC Number General Information Comment Organism
2.7.7.12 evolution GALT belongs to the histidine triad family of transferases Escherichia coli
2.7.7.12 evolution GALT belongs to the histidine triad family of transferases Homo sapiens
2.7.7.12 malfunction reduced galactose 1-phosphate uridylyltransferase activity is associated with the genetic disease type I galactosemia. Enzyme-deficiency results in an increase in the cellular concentration of galactose 1-phosphate. The accumulation of this toxic metabolite, combined with aberrant glycoprotein and glycolipid biosynthesis, is likely to be the major factor in molecular pathology Homo sapiens
2.7.7.12 metabolism the enzyme catalyzes a critical step in the Leloir pathway, overview Escherichia coli
2.7.7.12 metabolism the enzyme catalyzes a critical step in the Leloir pathway, overview Homo sapiens