Information on EC 1.1.1.133 - dTDP-4-dehydrorhamnose reductase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
1.1.1.133
-
RECOMMENDED NAME
GeneOntology No.
dTDP-4-dehydrorhamnose reductase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dTDP-beta-L-rhamnose + NADP+ = dTDP-4-dehydro-beta-L-rhamnose + NADPH + H+
show the reaction diagram
in the reverse direction, reduction on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme which catalyzes epimerization at C-3 and C-5; the complex has been referred to as dTDP-L-rhamnose synthase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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reduction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
dTDP-L-rhamnose biosynthesis
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dTDPLrhamnose biosynthesis
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Streptomycin biosynthesis
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Polyketide sugar unit biosynthesis
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Biosynthesis of antibiotics
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SYSTEMATIC NAME
IUBMB Comments
dTDP-6-deoxy-beta-L-mannose:NADP+ 4-oxidoreductase
In the reverse direction, reduction on the 4-position of the hexose moiety takes place only while the substrate is bound to another enzyme that catalyses epimerization at C-3 and C-5; the complex has been referred to as dTDP-L-rhamnose synthase.
CAS REGISTRY NUMBER
COMMENTARY hide
37250-64-9
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene L780
E3VXL5
UniProt
Manually annotated by BRENDA team
bifunctional 3,5-epimerase/4-keto reductase
Swissprot
Manually annotated by BRENDA team
O45
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-
Manually annotated by BRENDA team
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UniProt
Manually annotated by BRENDA team
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Manually annotated by BRENDA team
ATCC 7700
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
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Manually annotated by BRENDA team
Streptomyces mutans
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Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dTDP-4-dehydro-6-deoxy-D-glucose + NADH + H+
dTDP-beta-L-rhamnose + NAD+
show the reaction diagram
dTDP-4-dehydro-6-deoxy-D-glucose + NADPH
dTDP-beta-L-rhamnose + NADP+
show the reaction diagram
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-
-
?
dTDP-4-dehydro-6-deoxy-D-glucose + NADPH + H+
dTDP-L-rhamnose + NADP+
show the reaction diagram
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-
-
?
dTDP-6-deoxy-L-lyxo-4-hexulose + NAD(P)H
dTDP-L-rhamnose + NAD(P)+
show the reaction diagram
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-
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r
dTDP-6-deoxy-L-lyxo-4-hexulose + NADPH
dTDP-L-rhamnose + NADP+
show the reaction diagram
dTDP-6-deoxy-L-mannose + NADP+
dTDP-4-dehydro-6-deoxy-L-mannose + NADPH
show the reaction diagram
dTDP-alpha-D-glucose + NADP+
?
show the reaction diagram
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-
-
-
?
dTDP-beta-L-rhamnose + NADP+
dTDP-4-dehydro-beta-L-rhamnose + NADPH + H+
show the reaction diagram
UDP-4-dehydro-6-deoxy-D-glucose + NADPH
UDP-beta-L-rhamnose + NADP+
show the reaction diagram
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-
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?
UDP-4-keto-6-deoxy-D-glucose + NADPH + H+
UDP-L-rhamnose + NADP+
show the reaction diagram
E3VXL5;
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product identification by electrospray ionization-mass spectrometry and gas chromatography mass spectrometry
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?
additional information
?
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no substrate: GDP-4-keto-6-deoxy-mannose, UDP-glucose, dTDP-glucose, UDP-xylose, GDP-fucose
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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
dTDP-6-deoxy-L-lyxo-4-hexulose + NADPH
dTDP-L-rhamnose + NADP+
show the reaction diagram
dTDP-6-deoxy-L-mannose + NADP+
dTDP-4-dehydro-6-deoxy-L-mannose + NADPH
show the reaction diagram
dTDP-beta-L-rhamnose + NADP+
dTDP-4-dehydro-beta-L-rhamnose + NADPH + H+
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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situated at dimer interface
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,6,7-trihydroxy-9-(2-hydroxyphenyl)-3H-xanthen-3-one
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2,6,7-trihydroxy-9-methyl-3H-xanthen-3-one
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2,6,7-trihydroxy-9-phenyl-3H-xanthen-3-one
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5-ethenyl-1-methyl-9,10-dihydrophenanthrene-2,7-diol
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EDTA
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up to 0.3 mM, 70% loss of enzyme activity
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0169
dTDP-4-keto-6-deoxy-D-glucose
pH 8.5, 30°C
0.37
dTDP-alpha-D-glucose
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at pH 7.5, temperature not specified in the publication
0.106 - 0.21
NADH
0.009
NADPH
pH 8.5, 30°C
1.83
UDP-4-keto-6-deoxy-D-glucose
E3VXL5;
25°C, pH 7.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25
NADH
-
+/-48
29
NADPH
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+/-66
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0021
2,6,7-trihydroxy-9-(2-hydroxyphenyl)-3H-xanthen-3-one
Mycobacterium tuberculosis;
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pH and temperature not specified in the publication
0.0015
2,6,7-trihydroxy-9-methyl-3H-xanthen-3-one
Mycobacterium tuberculosis;
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pH and temperature not specified in the publication
0.0009
2,6,7-trihydroxy-9-phenyl-3H-xanthen-3-one
Mycobacterium tuberculosis;
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pH and temperature not specified in the publication
0.0025
5-ethenyl-1-methyl-9,10-dihydrophenanthrene-2,7-diol
Mycobacterium tuberculosis;
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pH and temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0011
E3VXL5;
25°C, pH 7.5
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5
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reduction of dTDP-6-deoxy-L-lyxo-4-hexulose
7.8
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assay at
10
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oxidation of dTDP-L-rhamnose
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45
about 35% of maximum activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
present in all tissues examined
Manually annotated by BRENDA team
PDB
SCOP
CATH
UNIPROT
ORGANISM
A0A1S0QL17
Bacillus anthracis;
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720);
Q9A0G6
Streptococcus pyogenes serotype M1;
Q96Z61
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7);
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
27500
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1 * 27500, SDS-PAGE
31900
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Y4 rmlD gene product, SDS-PAGE
32400
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NCTC 9710 rmlD gene product, SDS-PAGE
32540
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mass spectrometry, native protein
32560
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deduced from sequence
32600
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calculated from nucleotide sequence data
32730
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mass spectrometry, selenomethionine-enriched protein
33000
E3VXL5;
x * 33000, UGER, SDS-PAGE
34800
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SDS-PAGE
35000
x * 35500, deduced from gene sequence, x * 35000, SDS-PAGE
35500
x * 35500, deduced from gene sequence, x * 35000, SDS-PAGE
41500
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gel filtration
47000
E3VXL5;
gel filtration
49500
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light-scattering
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 35500, deduced from gene sequence, x * 35000, SDS-PAGE
monomer
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1 * 27500, SDS-PAGE; 1 * 32000, calculated from amino acid sequence
monomer or dimer
E3VXL5;
x * 33000, UGER, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
apo-enzyme, and in complex with NADH, NADPH or NADPH/dTDP-L-rhamnose
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sitting drop vapour-diffusion method, 6 d
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hanging drop vapor diffusion method, using 12.5% (w/v) PEG 1000, 12.5% (w/v) PEG 3350, 12.5% (v/v) 2-methyl-2,4-pentanediol, 0.02 M of each carboxylic acid (0.2 M sodium formate, 0.2 M ammonium acetate, 0.2 M trisodium citrate, 0.2 M sodium potassium L-tartrate, 0.2 M sodium oxamate) and 0.1 M MES/imidazole pH 6.5
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7
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37°C, 20 min, 75% activity loss
285846
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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stable below
37
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pH 7.0, 75% activity loss
42
E3VXL5;
stable for 30 min
50
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NADPH more than NADP+ prevents heat denaturation during 5 and 8 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
NADPH and to a lesser degree NADP+ prevent denaturation at 50°C, NAD+ and NADH are less effective
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 44% glycerol
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-20°C, purified protein, 50% glycerol
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-20°C, repeated freezing and thawing, loss of more than 60% of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
affinity and ion exchange chromatography
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ammonium sulfate precipitation, affinity chromatography, co-purification of enzyme I and II
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anion-exchange, hydrophobic chromatography
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HisTrap column chromatography and Superdex 75 gel filtration
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recombinant enzyme
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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gene L780, transcription profiling of UGER, phylogenetic analysis
E3VXL5;
gene rmlD, expression in Escherichia coli strain BL21(DE3)
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native overexpressed in Escherichia coli BL21(DE3) and selenomethionine-enriched in B834(lambdaDE3)
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overexpressed in Escherichia coli BL21(lambdaDE3)
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overexpression in Escherichia coli DH5alpha, ER2566, BL21(DE3)
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
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