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Information on EC 5.3.1.14 - L-rhamnose isomerase and Organism(s) Bacillus subtilis and UniProt Accession O05264

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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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Bacillus subtilis
UNIPROT: O05264
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Word Map
The taxonomic range for the selected organisms is: Bacillus subtilis
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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-
-
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L-rhamnose ketol-isomerase
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-
-
-
L-RI
-
-
-
-
RhaI
-
-
-
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Rhamnose isomerase
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
isomerization
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-
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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
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
D-allose
D-psicose
show the reaction diagram
-
-
-
r
D-psicose
D-allose
show the reaction diagram
-
-
-
r
D-ribose
D-ribulose
show the reaction diagram
-
-
-
r
L-Mannose
L-Fructose
show the reaction diagram
-
-
-
r
L-Rhamnose
L-Rhamnulose
show the reaction diagram
-
-
-
r
D-allose
D-psicose
show the reaction diagram
-
-
-
-
r
D-gulose
D-sorbose
show the reaction diagram
-
-
-
-
r
L-lyxose
L-xylulose
show the reaction diagram
-
-
-
-
r
L-Mannose
L-Fructose
show the reaction diagram
-
-
-
-
r
L-Rhamnose
L-Rhamnulose
show the reaction diagram
-
-
-
-
r
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Co2+
1 mM, 10fold activiation
Mg2+
1 mM, 2.9fold activiation
Mn2+
1 mM, 47fold activation
Mn2+
-
1 mM, 25fold increase in activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ba2+
1 mM, 68% inhibition
Ca2+
1 mM, 64% inhibition
Cu2+
1 mM, 45% inhibition
K+
1 mM, 68% inhibition
Na+
1 mM, 68% inhibition
Na2B4O7
1 mM, 90% inhibition
NH4+
1 mM, 67% inhibition
Zn2+
1 mM, 64% inhibition
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.98
D-allose
pH 8.5, 60°C
8.64
D-ribose
pH 8.5, 60°C
8
L-Mannose
pH 8.5, 60°C
0.49
L-rhamnose
pH 8.5, 60°C
86
L-Lyxose
-
pH 8.0, 60°C
97
L-Mannose
-
pH 8.0, 60°C
53
L-rhamnose
-
pH 8.0, 60°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.74
D-allose
pH 8.5, 60°C
30.7
D-ribose
pH 8.5, 60°C
10.5
L-Mannose
pH 8.5, 60°C
7.7
L-rhamnose
pH 8.5, 60°C
53
L-Lyxose
-
pH 8.0, 60°C
37
L-Mannose
-
pH 8.0, 60°C
153
L-rhamnose
-
pH 8.0, 60°C
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.12
D-allose
pH 8.5, 60°C
3.6
D-ribose
pH 8.5, 60°C
1.3
L-Mannose
pH 8.5, 60°C
15.75
L-rhamnose
pH 8.5, 60°C
0.62
L-Lyxose
-
pH 8.0, 60°C
0.38
L-Mannose
-
pH 8.0, 60°C
2.89
L-rhamnose
-
pH 8.0, 60°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.47
-
substrate L-allose, pH 8.0, 60°C
0.92
-
substrate L-mannose, pH 8.0, 60°C
2.58
-
substrate L-lyxose, pH 8.0, 60°C
3.58
-
substrate L-rhamnose, pH 8.0, 60°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
194000
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gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 48000, SDS-PAGE
tetramer
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4 * 48600, SDS-PAGE, 4 * 49468, calculated from sequence
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
60
4 h, 85% residual activity
70
-
2 h, 53% residual activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Bacillus subtilis
expression in Escherichia coli
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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40 g/l L-lyxose is produced from 100 g/l L-xylulose by the enzyme during 60 min, while 25 g/l L-mannose is produced from 100 g/l L-fructose in 80 min
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Park, C.
Characterization of a recombinant L-rhamnose isomerase from Bacillus subtilis and its application on production of L-lyxose and L-mannose
Biotechnol. Bioprocess Eng.
19
18-25
2014
Bacillus subtilis, Bacillus subtilis ATCC 23857
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Manually annotated by BRENDA team
Bai, W.; Shen, J.; Zhu, Y.; Men, Y.; Sun, Y.; Ma, Y.
Characteristics and kinetic properties of L-rhamnose isomerase from Bacillus subtilis by isothermal titration calorimetry for the production of D-allose
Food Sci. Technol. Res.
21
13-22
2015
Bacillus subtilis (O05264), Bacillus subtilis 168 (O05264)
-
Manually annotated by BRENDA team