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Information on EC 5.3.1.14 - L-rhamnose isomerase and Organism(s) Escherichia coli and UniProt Accession P32170

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IUBMB Comments
Contains two divalent metal ions located at different metal-binding sites within the active site. The enzyme binds the closed ring form of the substrate and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism. While the enzyme from the bacterium Escherichia coli is specific for L-rhamnose, the enzyme from the bacterium Pseudomonas stutzeri has broad substrate specificity and catalyses the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose .
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Escherichia coli
UNIPROT: P32170
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Word Map
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Synonyms
l-rhi, l-rhamnose isomerase, rhamnose isomerase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Isomerase, L-rhamnose
-
-
-
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L-rhamnose ketol-isomerase
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-
-
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L-RI
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-
-
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RhaI
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-
-
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Rhamnose isomerase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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intramolecular oxidoreduction
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-
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SYSTEMATIC NAME
IUBMB Comments
L-rhamnose aldose-ketose-isomerase
Contains two divalent metal ions located at different metal-binding sites within the active site. The enzyme binds the closed ring form of the substrate and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism. While the enzyme from the bacterium Escherichia coli is specific for L-rhamnose, the enzyme from the bacterium Pseudomonas stutzeri has broad substrate specificity and catalyses the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose [2].
CAS REGISTRY NUMBER
COMMENTARY hide
9023-84-1
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-lyxose
L-xylulose
show the reaction diagram
-
-
-
?
L-Mannose
L-Fructose
show the reaction diagram
-
-
-
-
r
L-Rhamnose
L-Rhamnulose
show the reaction diagram
additional information
?
-
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in mutants adapted to grow on L-lyxose: enzyme of the rhamnose metabolism and L-lyxose metabolism, inducable by L-rhamnose or L-lyxose
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-
?
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
additional information
?
-
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in mutants adapted to grow on L-lyxose: enzyme of the rhamnose metabolism and L-lyxose metabolism, inducable by L-rhamnose or L-lyxose
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
in the crystal structure, although not necessarily in vivo, rhamnose isomerase appears to bind Zn2+ at a structural site. In the presence of substrate the enzyme also binds Mn2+ at a nearby catalytic site
Zn2+
in the crystal structure, although not necessarily in vivo, rhamnose isomerase appears to bind Zn2+ at a structural site. In the presence of substrate the enzyme also binds Mn2+ at a nearby catalytic site
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5
L-Mannose
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L-lyxose
2
L-rhamnose
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1.7
L-rhamnulose
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
47000
-
x * 47000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 47000, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging-drop vapor diffusion method
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Noltmann, E.A.
Aldose-ketose isomerases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
6
271-354
1972
Escherichia coli, Escherichia coli B / ATCC 11303, Klebsiella aerogenes, Lactiplantibacillus plantarum, Yersinia pestis
-
Manually annotated by BRENDA team
Domagk, G.F.; Zech, R.
L-Rhamnose isomerase
Methods Enzymol.
9
579-582
1966
Escherichia coli, Lactiplantibacillus plantarum, Yersinia pestis
-
Manually annotated by BRENDA team
Garcia-Junceda, E.; Shen, G.J.; Alajarin, R.; Wong, C.H.
Cloning and overexpression of rhamnose isomerase and fucose isomerase
Bioorg. Med. Chem.
3
1349-1355
1995
Escherichia coli
Manually annotated by BRENDA team
Badia, J.; Baldoma, L.; Aguilar, J.; Boronat, A.
Identification of the rhaA, rhaB and rhaD gene products from Escherichia coli K-12
FEMS Microbiol. Lett.
65
253-258
1989
Escherichia coli
Manually annotated by BRENDA team
Badia, J.; Gimenez, R.; Baldoma, L.; Barnes, E.; Fessner, W.D.; Aguilar, J.
L-Lyxose metabolism employs the L-rhamnose pathway in mutant cells of Escherichia coli adapted to grow on L-lyxose
J. Bacteriol.
173
5144-5150
1991
Escherichia coli
Manually annotated by BRENDA team
Korndrfer, I.P.; Fessner, W.D.; Matthews, B.W.
The structure of rhamnose isomerase from Escherichia coli and its relation with xylose isomerase illustrates a change between inter and intra-subunit complementation during evolution
J. Mol. Biol.
300
917-933
2000
Escherichia coli (P32170), Escherichia coli
Manually annotated by BRENDA team