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Information on EC 1.1.1.133 - dTDP-4-dehydrorhamnose reductase and Organism(s) Pseudomonas aeruginosa

for references in articles please use BRENDA:EC1.1.1.133

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IUBMB Comments

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.

The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms

Synonyms
4-ketoreductase, agl14, dtdp-4-dehydrorhamnose reductase, dtdp-6-deoxy-l-lyxo-4-hexulose reductase, dtdp-4-keto-l-rhamnose reductase, dtdp-4-keto-rhamnose reductase, thymidine diphosphate-4-dehydrorhamnose reductase, more

SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dTDP-4-keto-L-rhamnose reductase
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-
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dTDP-4-ketorhamnose reductase
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-
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dTDP-6-deoxy-L-mannose dehydrogenase
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-
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dTDP-L-rhamnose synthetase
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-
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TDP-4-keto-rhamnose reductase
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-
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TDP-4-ketorhamnose reductase
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-
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thymidine diphospho-4-ketorhamnose reductase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
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redox reaction
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-
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reduction
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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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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY hide
Reversibility
r=reversible
ir=irreversible
?=not specified
dTDP-4-dehydro-6-deoxy-D-glucose + NADPH + H+
dTDP-L-rhamnose + NADP+
show the reaction diagram
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Substrates: -
Products: -
?
top print hide Go to Organism Search
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
ATCC 7700
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Manually annotated by BRENDA team
Highest Expressing Human Cell Lines
Cell Line Links Gene Links
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A0A0F7QGS2_PSEAI
294
0
32940
TrEMBL
other Location (Reliability: 4)
A0A241XVW0_PSEAI
302
0
33089
TrEMBL
-
A0A367MFS2_PSEAI
302
0
33169
TrEMBL
-
A0A3P3E7G6_PSEAI
302
0
33113
TrEMBL
-
A0A509JIE2_PSEAI
302
0
33050
TrEMBL
-
A0A5E5R7N2_PSEAI
294
0
32949
TrEMBL
-
A0A6A9K5Y4_PSEAI
302
0
33047
TrEMBL
-
A0A6B1YAU2_PSEAI
302
0
33098
TrEMBL
-
A0A7M2ZZQ7_PSEAI
302
0
33117
TrEMBL
-
A0A9P1W1R4_PSEAI
302
0
33118
TrEMBL
-
A0AAQ3LK25_PSEAI
302
0
33114
TrEMBL
-
A0ABD7JSY8_PSEAI
294
0
32939
TrEMBL
-
A0ABD7K0W2_PSEAI
302
0
33148
TrEMBL
other Location (Reliability: 2)
G3XCK0_PSEAI
302
0
33107
TrEMBL
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, affinity chromatography, co-purification of enzyme I and II
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Melo, A.; Glaser, L.
The mechanism of 6-deoxyhexose synthesis. II. Conversion of deoxythymidine diphosphate 4-keto-6-deoxy-D-glucose to deoxythymidine diphosphate L-rhamnose
J. Biol. Chem.
243
1475-1478
1968
Pseudomonas aeruginosa
Manually annotated by BRENDA team