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Information on EC 5.1.3.3 - Aldose 1-epimerase and Organism(s) Homo sapiens and UniProt Accession Q96C23
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5.1.3.3 Aldose 1-epimeraseIUBMB Comments
Also acts on L-arabinose, D-xylose, D-galactose, maltose and lactose. This enzyme catalyses the first step in galactose metabolism by converting beta-D-galactose into alpha-D-galactose, which is the substrate for EC 2.7.1.6, galactokinase [5,6].
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Word Map
- 5.1.3.3
-
anomer
-
mutarotation
-
leloir
-
beta-anomers
- alpha-d-galactose
- beta-d-galactose
- galactokinase
- alpha-d-glucose
-
gale
- analysis
- synthesis
The taxonomic range for the selected organisms is: Homo sapiens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
mutarotase, galactose mutarotase, aldose 1-epimerase, aldose-1-epimerase, styead, aldose-l-epimerase, galactomutarotase, aldose mutarotase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aldose mutarotase
-
-
-
-
Epimerase, aldose-1
-
-
-
-
Mutarotase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha-D-glucose = beta-D-glucose
E307 and H176 may act as catalytic acid and catalytic base, respectively
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
epimerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
Aldose 1-epimerase
Also acts on L-arabinose, D-xylose, D-galactose, maltose and lactose. This enzyme catalyses the first step in galactose metabolism by converting beta-D-galactose into alpha-D-galactose, which is the substrate for EC 2.7.1.6, galactokinase [5,6].
CAS REGISTRY NUMBER
COMMENTARY
182938-11-0
-
9031-76-9
-
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
additional information
?
-
key enzyme of carbohydrate metabolism catalysing the interconversion of the alpha-anomer and beta-anomer of hexose sugars such as glucose and galactose
-
?
additional information
?
-
-
key enzyme of carbohydrate metabolism catalysing the interconversion of the alpha-anomer and beta-anomer of hexose sugars such as glucose and galactose
-
?
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
additional information
?
-
key enzyme of carbohydrate metabolism catalysing the interconversion of the alpha-anomer and beta-anomer of hexose sugars such as glucose and galactose
-
?
additional information
?
-
-
key enzyme of carbohydrate metabolism catalysing the interconversion of the alpha-anomer and beta-anomer of hexose sugars such as glucose and galactose
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). GALM_HUMAN
342
0
37766
Swiss-Prot
other Location (Reliability: 3)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme undergoes a molecular transition to a more compact form
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
both apoform and in complex with beta-D-galactose, comparison with enzyme from Lactococcus lactis and Caenorhabditis elegans
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H107A
mutant enzyme with 5fold reduced activity with alpha-D-galactose and 7.8fold reduced activity with alpha-D-glucose, compared to wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Mulhern, S.A.; Fishman, P.H.; Kusiak, J.W.; Bailey, J.M.
Physical characteristics and chemi-osmotic transformations of mutarotases from various species
J. Biol. Chem.
248
4163-4173
1973
Batrachoididae gen. sp., Bos taurus, Canis lupus familiaris, Capsicum frutescens, Catfish, Cavia porcellus, Escherichia coli, Gallus gallus, Homo sapiens, Lithobates catesbeianus, Meriones unguiculatus, Mus musculus, Mushroom, Oryctolagus cuniculus, Ovis aries, Perca flavescens, Sus scrofa
Bailey, J.M.; Fishman, P.H.; Kusiak, J.W.; Mulhern, S.; Pentchev, P.G.
Mutarotase (aldose 1-epimerase) from kidney cortex
Methods Enzymol.
41
471-484
1975
Bos taurus, Capsicum frutescens, Catfish, Escherichia coli, Gallus gallus, Homo sapiens, Lithobates catesbeianus, Mushroom, Oryctolagus cuniculus, Ovis aries
Timson, D.J.; Reece, R.J.
Identification and characterisation of human aldose 1-epimerase
FEBS Lett.
543
21-24
2003
Homo sapiens (Q96C23), Homo sapiens
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