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Information on EC 5.1.3.32 - L-rhamnose mutarotase and Organism(s) Escherichia coli and UniProt Accession P32156

for references in articles please use BRENDA:EC5.1.3.32
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EC Tree
     5 Isomerases
         5.1 Racemases and epimerases
             5.1.3 Acting on carbohydrates and derivatives
                5.1.3.32 L-rhamnose mutarotase
IUBMB Comments
The enzyme is specific for L-rhamnopyranose.
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This record set is specific for:
Escherichia coli
UNIPROT: P32156
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Synonyms
l-rhamnose mutarotase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
rhamnose 1-epimerase
-
type-3 mutarotase
-
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-rhamnopyranose 1-epimerase
The enzyme is specific for L-rhamnopyranose.
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 SUBSTRATE
NATURAL 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
-
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
gene deletion leads o decreased growth rate only in the presence of low concentrations of L-rhamnose, with no difference in growth rate between the wild-type and mutant strains when the concentration of L-rhamnose in the media is 0.2%. The maximum amount of growth and the lag phase time of the wild-type strain are higher and shorter, respectively, compared with those of the mutant
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
the enzyme seems to require multimeric or dimeric structure for their enzymatic activity
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H22A
mutant does not fold properly
H22K
mutant does not fold properly
Y18A
mutant does not fold properly
Y18E
mutant does not fold properly
Y18F
binding affinity for L-rhamnose is comparable to that of the wild-type, no catalytic activity
Y18H
mutant does not fold properly
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ryu, K.S.; Kim, C.; Kim, I.; Yoo, S.; Choi, B.S.; Park, C.
NMR application probes a novel and ubiquitous family of enzymes that alter monosaccharide configuration
J. Biol. Chem.
279
25544-25548
2004
Escherichia coli (P32156)
Manually annotated by BRENDA team
Ryu, K.S.; Kim, J.I.; Cho, S.J.; Park, D.; Park, C.; Cheong, H.K.; Lee, J.O.; Choi, B.S.
Structural insights into the monosaccharide specificity of Escherichia coli rhamnose mutarotase
J. Mol. Biol.
349
153-162
2005
Escherichia coli (P32156)
Manually annotated by BRENDA team