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Information on EC 5.1.3.2 - UDP-glucose 4-epimerase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P04397
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5.1.3.2 UDP-glucose 4-epimeraseIUBMB Comments
Requires NAD+. Also acts on UDP-2-deoxyglucose.
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Word Map
- 5.1.3.2
- polysaccharide
- galactokinase
-
leloir
- galactosemia
- galactose-1-phosphate
- udp-galnac
- udp-n-acetylglucosamine
-
galactose-inducible
-
kluyveromyces
-
pyrophosphorylase
- fragilis
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uridylyltransferase
- udp-n-acetylgalactosamine
- udpglucose
- udp-sugars
- galnac
- mutarotase
-
galactose-containing
-
o-antigens
-
udp-glucuronic
- medicine
- synthesis
The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
gal10, udp-galactose 4-epimerase, 4-epimerase, udp-glucose 4-epimerase, udp-galactose-4-epimerase, udp-galactose 4'-epimerase, udp-glucose 4'-epimerase, udp-glucose-4-epimerase, udp-glucose epimerase, gal10p, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-Epimerase
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-
-
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Epimerase, uridine diphosphoglucose
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-
-
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Gal10p
Galactowaldenase
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-
-
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UDP-D-galactose 4-epimerase
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-
-
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UDP-galactose 4-epimerase
UDP-glucose epimerase
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-
-
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UDPG-4-epimerase
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-
-
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UDPgalactose 4-epimerase
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-
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Uridine diphosphate galactose 4-epimerase
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-
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Uridine diphosphate glucose 4-epimerase
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-
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Uridine diphospho-galactose-4-epimerase
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-
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Uridine diphosphoglucose 4-epimerase
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-
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Uridine diphosphoglucose epimerase
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Gal10p
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the first and the last enzyme of the Leloir pathway, galactose mutarotase and UDP-galactose 4-epimerase, are comtained within a single polypeptide chain referred to as Gal10p
UDP-galactose 4-epimerase
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-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose = UDP-alpha-D-galactose
reaction mechanism, overview
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
UDP-glucose 4-epimerase
Requires NAD+. Also acts on UDP-2-deoxyglucose.
CAS REGISTRY NUMBER
COMMENTARY
9032-89-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-galactose
UDP-glucose
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Leloir pathway of D-galactose catabolism
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-
?
UDP-galactose
UDP-glucose
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Leloir pathway of galactose metabolism
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-
r
additional information
?
-
the bifunctional enzyme GAL10 also exhibits galactose mutarotase activity, EC 5.1.3.3
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-
?
additional information
?
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UDPgalactose 4-epimerase is a bifunctional enzyme with aldose 1-epimerase activity. The epimerase and mutarotase activities are located in different regions of the epimerase holoenzyme
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-galactose
UDP-glucose
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Leloir pathway of D-galactose catabolism
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-
?
UDP-galactose
UDP-glucose
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Leloir pathway of galactose metabolism
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-
r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5'-UMP
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epimerase activity is completely lost but mutarotase activity remains unaffected after treatement with 5'-UMP and L-arabinose
L-arabinose
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epimerase activity is completely lost but mutarotase activity remains unaffected after treatement with 5'-UMP and L-arabinose
L-Arabinose plus UMP or UDP
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inactivation due to reduction of the epimerase NAD+
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L-Xylose plus UMP or UDP
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inactivation due to reduction of the epimerase NAD+
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.6
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GALE activity evaluated in samples by monitoring the conversion of UDP-gal to UDP-glc. Assays stopped by the addition of 237.5 microliter of ice-cold water followed immediately by filtration through 0.2-micrometer nylon micro-spin columns (Corning) to remove proteins and particulates before high performance liquid chromatography analysis.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.7 - 8.1
-
6.7: 91% of maximal activity, 8.1: 88% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
UDP-Gal 4-epimerases and the other GalE-like UDP-sugar 4-epimerases belong to the short-chain dehydrogenase/reductase (SDR) superfamily of proteins. Classification of UDP-hexose 4-epimerases into three groups with distinct substrate promiscuity. Group 1 contains the 4-epimerases that exhibit a strong preference for non-acetylated substrates (such as Escherichia coli enzyme eGalE), group 2 members can epimerize both non-acetylated and N-acetylated substrates equally well (such as the human enzyme hGalE), and group 3 epimerases are very specific for N-acetylated substrates (like the WbpP from Pseudomonas aeruginosa)
metabolism
UDP-sugar 4-epimerase (GalE) is one of enzymes in the Leloir pathway
physiological function
UDP-galactose 4-epimerase is important for the biosynthesis of polysaccharide structures
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
183000 - 187000
-
sucrose density gradient centrifugation, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion methodthree-dimensional structure of gal10p in complex with NAD+, UDP-glucose, and beta-D-galactose is determined to 1.85 A resolution. Space group I222 with unit cell dimensions of a = 120.9 A, b = 125.2 A and c = 142.3 A. The asymmetric unit contains one monomer
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
30
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53% loss of activity within 20 min, partial protection by NAD+, up to a concentration of 7 mM
30
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53% loss of activity within 10 min, partial protection by NAD+, up to a concentration of 7 mM
37
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85% loss of activity within 20 min, partial protection by NAD+, up to a concentration of 7 mM
37
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85% loss of activity within 20 min, partial protection by NAD+, up to a concentration of 7 mM. Partial protection by addition of NAD+ up to a concentration of 1 mM
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
To explore the quantitative relationship between GALE activity and galactose metabolism and sensitivity in yeast, a strain is generated in which the expression of GAL10, encoding GALE, was regulated by doxycycline. In brief, a doxycycline-repressible promoter is introduced just upstream of the GAL10 coding sequence in a strain (JFy4763) that was otherwise wild type for all Leloir pathway enzymes and that was engineered to express the appropriate doxycycline-responsive transcriptional activator and repressor protein moieties.
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Fukasawa, T.; Segawa, T.; Nogi, Y.
Uridine diphosphate glucose-4-epimerase and galactose-1-phosphate uridylyltransferase from Saccharomyces cerevisiae
Methods Enzymol.
89
584-592
1982
Saccharomyces cerevisiae
Fukasawa, T.; Obonai, K.; Segawa, T.; Nogi, Y.
The enzymes of the galactose cluster in Saccharomyces cerevisiae. II. Purification and characterization of uridine diphosphoglucose 4-epimerase
J. Biol. Chem.
255
2705-2707
1980
Saccharomyces cerevisiae
Carmenes, R.S.; Gascon, S.; Moreno, F.
Mechanism of inactivation of UDP-glucose 4-epimerase from Saccharomyces cerevisiae by D-xylose and L-arabinose
Yeast
2
101-108
1986
Saccharomyces cerevisiae
Majumdar, S.; Ghatak, J.; Mukherji, S.; Bhattacharjee, H.; Bhaduri, A.
UDPgalactose 4-epimerase from Saccharomyces cerevisiae. A bifunctional enzyme with aldose 1-epimerase activity
Eur. J. Biochem.
271
753-759
2004
Saccharomyces cerevisiae
Thoden, J.B.; Holden, H.M.
The molecular architecture of galactose mutarotase/UDP-galactose 4-epimerase from Saccharomyces cerevisiae
J. Biol. Chem.
280
21900-21907
2005
Saccharomyces cerevisiae
Scott, A.; Timson, D.J.
Characterization of the Saccharomyces cerevisiae galactose mutarotase/UDP-galactose 4-epimerase protein, Gal10p
FEMS Yeast Res.
7
366-371
2007
Saccharomyces cerevisiae
Wasilenko, J.; Fridovich-Keil, J.L.
Relationship between UDP-galactose 4-epimerase activity and galactose sensitivity in yeast
J. Biol. Chem.
281
8443-8449
2006
Saccharomyces cerevisiae
Beerens, K.; Soetaert, W.; Desmet, T.
UDP-hexose 4-epimerases a view on structure, mechanism and substrate specificity
Carbohydr. Res.
414
8-14
2015
Marinithermus hydrothermalis (F2NQX6), Thermus thermophilus (F6DEY6), Saccharomyces cerevisiae (P04397), Escherichia coli (P09147), Streptococcus thermophilus (P21977), Homo sapiens (Q14376), Homo sapiens, Drosophila melanogaster (Q9W0P5), Saccharomyces cerevisiae ATCC 204508 / S288c (P04397), Thermus thermophilus SG0.5JP17-16 (F6DEY6), Marinithermus hydrothermalis DSM 14884 / JCM 11576 / T1 (F2NQX6)
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