Information on EC 5.1.3.32 - L-rhamnose mutarotase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
5.1.3.32
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RECOMMENDED NAME
GeneOntology No.
L-rhamnose mutarotase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha-L-rhamnopyranose = beta-L-rhamnopyranose
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
L-rhamnose degradation I
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SYSTEMATIC NAME
IUBMB Comments
L-rhamnopyranose 1-epimerase
The enzyme is specific for L-rhamnopyranose.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha-L-rhamnopyranose
beta-L-rhamnopyranose
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha-L-rhamnopyranose
beta-L-rhamnopyranose
show the reaction diagram
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
12000
2 * 12000 and 2 * 14000, SDS-PAGE, 2 * 16595, mass spectrometry, 2 * 16595,calculated
14000
2 * 12000 and 2 * 14000, SDS-PAGE, 2 * 16595, mass spectrometry, 2 * 16595,calculated
16595
2 * 12000 and 2 * 14000, SDS-PAGE, 2 * 16595, mass spectrometry, 2 * 16595,calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
2 * 12000 and 2 * 14000, SDS-PAGE, 2 * 16595, mass spectrometry, 2 * 16595,calculated
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
in complex with L-rhamnose, to 1.8 A resolution. Protein is a locally asymmetric dimer and has a preference for the beta-form of L-rhamnose
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to 1.6 A resolution. Structure shows a dimer in the asymmetric unit with a very similar structure to that of L-rhamnose mutarotase YiiL of Escherichia coli
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expresssion in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H22A
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mutant does not fold properly
H22K
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mutant does not fold properly
Y18A
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mutant does not fold properly
Y18E
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mutant does not fold properly
Y18F
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binding affinity for L-rhamnose is comparable to that of the wild-type, no catalytic activity
Y18H
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mutant does not fold properly
Show AA Sequence (1796 entries)
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