Information on EC 5.1.3.13 - dTDP-4-dehydrorhamnose 3,5-epimerase

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The expected taxonomic range for this enzyme is: dsDNA viruses, no RNA stage, Bacteria, Archaea

EC NUMBER
COMMENTARY
5.1.3.13
-
RECOMMENDED NAME
GeneOntology No.
dTDP-4-dehydrorhamnose 3,5-epimerase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-beta-L-mannose
show the reaction diagram
-
-
-
-
dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-beta-L-mannose
show the reaction diagram
dTDP-4-keto-L-rhamnose is formed as intermediate
-
dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-4-dehydro-6-deoxy-beta-L-mannose
show the reaction diagram
dTDP-4-keto-L-rhamnose is formed as intermediate
Escherichia coli Y10
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
epimerization
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Biosynthesis of secondary metabolites
-
dTDP-beta-L-noviose biosynthesis
-
dTDP-L-rhamnose biosynthesis I
-
Metabolic pathways
-
Polyketide sugar unit biosynthesis
-
Streptomycin biosynthesis
-
SYSTEMATIC NAME
IUBMB Comments
dTDP-4-dehydro-6-deoxy-D-glucose 3,5-epimerase
The enzyme occurs in a complex with EC 1.1.1.133 dTDP-4-dehydrorhamnose reductase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
bifunctional UDP-4-keto-6-deoxy-D-glucose epimerase/reductase
E3VXL5
-
deoxythymidine diphosphate-4-dehydrorhamnose 3,5-epimerase
Gluconacetobacter xylinus
-
-
dTDP-4-dehydrorhamnose 3,5-epimerase
Gluconacetobacter xylinus
-
-
dTDP-4-keto-6-deoxy-D-hexulose 3,5-epimerase
-
-
dTDP-4-keto-6-deoxyglucose 3,5-epimerase
-
-
-
-
dTDP-4-keto-L-rhamnose 3,5-epimerase
-
-
-
-
dTDP-6-deoxy-D-xylo-4-hexulose 3',5'-epimerase
-
-
dTDP-L-rhamnose synthetase
-
-
-
-
Epimerase, thymidine diphospho-4-ketorhamnose 3,5-
-
-
-
-
NovW gene product
-
-
RmlC
O05369
previously RfbD
TDP-4-keto-6-deoxy-D-glucose 3,5-epimerase
O05369
-
TDP-4-keto-L-rhamnose-3,5-epimerase
-
-
-
-
TDP-4-ketorhamnose 3,5-epimerase
-
-
-
-
TDP-6-deoxy-D-xylo-4-hexopyranosid-4-ulose 3,5-epimerase
-
-
Thymidine diphospho-4-ketorhamnose 3,5-epimerase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
37318-39-1
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
gene L780
E3VXL5
UniProt
Manually annotated by BRENDA team
strain 045
-
-
Manually annotated by BRENDA team
strain Y10
-
-
Manually annotated by BRENDA team
Escherichia coli 45
strain 045
-
-
Manually annotated by BRENDA team
Escherichia coli Y10
strain Y10
-
-
Manually annotated by BRENDA team
Gluconacetobacter xylinus
mutant strain K3, isolated from Kombucha, Kombu Australia, Springwood, Queensland, Australia
-
-
Manually annotated by BRENDA team
serovar typhimurium
-
-
Manually annotated by BRENDA team
serovar typhimurium LT2
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
O05369
rhamnose and N-acetyl-galactosamine are not detected, and fucose is greatly diminished in the rmlC mutant (transposon pLOF/Sp inserted into rmlC (TDP-4-keto-6-deoxy-D-glucose 3,5-epimerase) compared with that in the wild-type strain)
metabolism
Gluconacetobacter xylinus
-
dTDP-4-dehydrorhamnose 3,5-epimerase is an enzyme which may be associated with the cellulose synthesis-reducing effect of the mutation in strain K3
metabolism
O05369
the enzyme is required for L-rhamnose synthesis
physiological function
O05369
the rmlC mutant strain colonizes the rabbit mitral valves approximately 3fold less effectively than the wild type strain
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dTDP-4-dehydro-6-deoxy-D-glucose
dTDP-4-dehydro-6-deoxy-L-mannose
show the reaction diagram
-
-
-
-
dTDP-4-dehydro-6-deoxy-D-glucose
dTDP-4-dehydro-6-deoxy-L-mannose
show the reaction diagram
-
-
-
-
dTDP-4-dehydro-6-deoxy-D-glucose
dTDP-4-dehydro-6-deoxy-L-mannose
show the reaction diagram
-
-
-
-
dTDP-4-dehydro-6-deoxy-D-glucose
dTDP-4-dehydro-6-deoxy-L-mannose
show the reaction diagram
Escherichia coli Y10
-
-
-
-
dTDP-4-dehydro-6-deoxy-D-glucose
?
show the reaction diagram
-
enzyme in biosynthesis of dTDP-L-dihydrostreptose from dTDP-6-deoxy-D-xylo-4-hexosulose
-
-
-
dTDP-4-dehydro-6-deoxy-D-glucose
dTDP-4-dehydro-L-rhamnose
show the reaction diagram
Gluconacetobacter xylinus
-
-, the enzyme is involved in the dTDP-rhamnose synthesis pathway which consists of three steps: (i) the synthesis of dTDP-4-keto-6-deoxy-D-glucose from glucose 1-phosphate and dTDP, (ii) the conversion of dTDP-4-keto-6-deoxy-D-glucose to dTDP-4-keto-L-rhamnose by dTDP-4-dehydrorhamnose 3,5-epimerase and (iii) the reduction of dTDP-4-keto-L-rhamnose to dTDP-L-rhamnose. The mutant K3 strain, with a spontaneous mutation that results in lower cellulose production, shows deoxythymidine diphosphate-4-dehydrorhamnose 3,5-epimerase activity, while the wild-type does not, determined by 2D-gel electrophoresis. It is possible that in the wild-type, transcription of the gene responsible for the expression of dTDP-4-dehydrorhamnose 3,5-epimerase is repressed by a transcription factor, and that a mutation in the gene encoding the transcription factor has rendered it non-functional
-
-
?
dTDP-6-deoxy-D-xylo-4-hexulose
dTDP-6-deoxy-L-lyxo-4-hexulose
show the reaction diagram
-
-
-
?
TDP-6-deoxy-D-xylo-4-hexosulose
TDP-6-deoxy-L-lyxo-4-hexosulose
show the reaction diagram
-
-
-
-
TDP-6-deoxy-D-xylo-4-hexosulose
TDP-6-deoxy-L-lyxo-4-hexosulose
show the reaction diagram
-
-
-
-
TDP-6-deoxy-D-xylo-4-hexosulose
?
show the reaction diagram
-
enzyme in biosynthesis of the cell wall component 6-deoxy-L-talose
-
-
-
TDP-6-deoxy-D-xylo-4-hexosulose
?
show the reaction diagram
-
enzyme in biosynthesis of dTDP-L-rhamnose from dTDP-D-glucose
-
-
-
TDP-6-deoxy-D-xylo-4-hexosulose
?
show the reaction diagram
-
enzyme is required for biosynthesis of the daunorubicin precursor thymidine diphospho-L-daunosamine
-
-
-
TDP-6-deoxy-D-xylo-4-hexosulose
?
show the reaction diagram
Escherichia coli 45
-
enzyme in biosynthesis of the cell wall component 6-deoxy-L-talose
-
-
-
TDP-6-deoxy-D-xylo-hexopyranosid-4-ulose
TDP-L-rhamnose
show the reaction diagram
-, O06330
conversion of TDP-6-deoxy-D-xylo-hexopyranosid-4-ulose to TDP-L-rhamnose, catalyzed by the two enzymes TDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase, RmlC, and TDP-deoxy-L-lyxo-4-hexulose reductase, RmlD, overview
-
-
?
UDP-4-dehydro-6-deoxy-D-glucose
UDP-4-dehydro-6-deoxy-L-mannose
show the reaction diagram
E3VXL5
-
i.e. UDP-4-dehydro-L-rhamnose, product identification by electrospray ionization-mass spectrometry and gas chromatography mass spectrometry
-
?
dTDP-6-deoxy-D-xylo-4-hexulose
dTDP-6-deoxy-L-lyxo-4-hexulose
show the reaction diagram
-
third enzyme of the rhamnose pathway
-
-
?
additional information
?
-
-
the enzyme is involved in the biosynthesis of dTDP-L-rhamnose, which is an essential component of the bacterial cell wall
-
?
additional information
?
-
-
the enzyme is required for dTDP-L-rhamnose biosynthesis
-
?
additional information
?
-
-
third enzyme of dTDP-L-rhamnose pathway
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dTDP-4-dehydro-6-deoxy-D-glucose
?
show the reaction diagram
-
enzyme in biosynthesis of dTDP-L-dihydrostreptose from dTDP-6-deoxy-D-xylo-4-hexosulose
-
-
-
dTDP-4-dehydro-6-deoxy-D-glucose
dTDP-4-dehydro-L-rhamnose
show the reaction diagram
Gluconacetobacter xylinus
-
the enzyme is involved in the dTDP-rhamnose synthesis pathway which consists of three steps: (i) the synthesis of dTDP-4-keto-6-deoxy-D-glucose from glucose 1-phosphate and dTDP, (ii) the conversion of dTDP-4-keto-6-deoxy-D-glucose to dTDP-4-keto-L-rhamnose by dTDP-4-dehydrorhamnose 3,5-epimerase and (iii) the reduction of dTDP-4-keto-L-rhamnose to dTDP-L-rhamnose. The mutant K3 strain, with a spontaneous mutation that results in lower cellulose production, shows deoxythymidine diphosphate-4-dehydrorhamnose 3,5-epimerase activity, while the wild-type does not, determined by 2D-gel electrophoresis. It is possible that in the wild-type, transcription of the gene responsible for the expression of dTDP-4-dehydrorhamnose 3,5-epimerase is repressed by a transcription factor, and that a mutation in the gene encoding the transcription factor has rendered it non-functional
-
-
?
TDP-6-deoxy-D-xylo-4-hexosulose
?
show the reaction diagram
-
enzyme in biosynthesis of the cell wall component 6-deoxy-L-talose
-
-
-
TDP-6-deoxy-D-xylo-4-hexosulose
?
show the reaction diagram
-
enzyme in biosynthesis of dTDP-L-rhamnose from dTDP-D-glucose
-
-
-
TDP-6-deoxy-D-xylo-4-hexosulose
?
show the reaction diagram
-
enzyme is required for biosynthesis of the daunorubicin precursor thymidine diphospho-L-daunosamine
-
-
-
TDP-6-deoxy-D-xylo-4-hexosulose
?
show the reaction diagram
Escherichia coli 45
-
enzyme in biosynthesis of the cell wall component 6-deoxy-L-talose
-
-
-
TDP-6-deoxy-D-xylo-hexopyranosid-4-ulose
TDP-L-rhamnose
show the reaction diagram
-, O06330
conversion of TDP-6-deoxy-D-xylo-hexopyranosid-4-ulose to TDP-L-rhamnose, catalyzed by the two enzymes TDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase, RmlC, and TDP-deoxy-L-lyxo-4-hexulose reductase, RmlD, overview
-
-
?
dTDP-6-deoxy-D-xylo-4-hexulose
dTDP-6-deoxy-L-lyxo-4-hexulose
show the reaction diagram
-
third enzyme of the rhamnose pathway
-
-
?
additional information
?
-
-
the enzyme is required for dTDP-L-rhamnose biosynthesis
-
?
additional information
?
-
-
third enzyme of dTDP-L-rhamnose pathway
-
?
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
additional information
-
no cofactors are required
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
E3VXL5
divalent metal ions do not alter activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1-(3-(5-allyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylsulfonyl)-propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
-
1-(3-(5-allyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
i.e. 77074, a SID 7975595 analogue
1-(3-(5-allyl-8-methyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
-
1-(3-(5-ethyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylsulfonyl)-propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
-
1-(3-(5-ethyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
i.e. SID 7975595, a competitive, fast-on rate, fully reversible inhibitor of RmlC. Increases the Km for TDP-6-deoxy-D-xylo-hexopyranosid-4-ulose. Cytotoxic SID 7975595 has an IC50 of approximately 0.075 mM in HAE cells
-
1-(3-(5-methyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
i.e. 77072, a SID 7975595 analogue
1-(3-(5-methylphenyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
i.e. 77070, a SID 7975595 analogue
1-(3-(5-propyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
i.e. 77071, a SID 7975595 analogue
1-(3-(5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
i.e. 77073, a SID 7975595 analogue
additional information
-, O06330
modeling of triazinoindol-benzimidazolones into the active site of RmlC, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.025
-
dTDP-4-dehydro-6-deoxy-D-glucose
-
-
0.35
-
dTDP-6-deoxy-D-xylo-4-hexulose
-
RmlC K73A
0.48
-
dTDP-6-deoxy-D-xylo-4-hexulose
-
RmlC Y133F
0.71
-
dTDP-6-deoxy-D-xylo-4-hexulose
-
pH 7.0, 25C
0.71
-
dTDP-6-deoxy-D-xylo-4-hexulose
-
native
additional information
-
additional information
-
-
-
additional information
-
additional information
-, O06330
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.016
-
dTDP-6-deoxy-D-xylo-4-hexulose
-
RmlC Y133F
0.095
-
dTDP-6-deoxy-D-xylo-4-hexulose
-
RmlC K73A
39
-
dTDP-6-deoxy-D-xylo-4-hexulose
-
pH 7.0, 25C
39
-
dTDP-6-deoxy-D-xylo-4-hexulose
-
native
additional information
-
additional information
-
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0004
-
1-(3-(5-allyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylsulfonyl)-propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
pH 7.4, 25C
0.00012
-
1-(3-(5-allyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
-
0.02
-
1-(3-(5-allyl-8-methyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
-
0.0008
-
1-(3-(5-ethyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylsulfonyl)-propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
pH 7.4, 25C
0.0002
-
1-(3-(5-ethyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
pH 7.4, 25C
-
0.0005
-
1-(3-(5-methyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
pH 7.4, 25C
0.0029
-
1-(3-(5-methylphenyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
pH 7.4, 25C
0.00125
-
1-(3-(5-propyl-5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
pH 7.4, 25C
0.0033
-
1-(3-(5H-[1,2,4]triazino[5,6-b]indol-3-ylthio)propyl)-1H-benzo[d]imidazol-2(3H)-one
-, O06330
pH 7.4, 25C
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.4
-
-, O06330
assay at
7.5
8.5
-
-
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
-, O06330
assay at
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
Sulfolobus tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
40600
-
-
gel filtration
47000
-
E3VXL5
gel filtration
67000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
-
each monomer is formed mainly from two beta-sheets arranged in a beta-sandwich. The structure of a dTDP-phenol-enzyme complex shows the substrate-binding site to be located between the two beta-sheets, this site is formed from residues of both monomers
monomer
-
1 * 40000, SDS-PAGE
monomer or dimer
E3VXL5
x * 33000, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
hanging drop vapor diffusion method, crystal structure in presence and absence of dTDP
-
incubating RmlC with 20 mM dTDP-6-deoxy-D-xylo-4-hexulose, for 2 h at room temperature, prior to setting up crystal plates with 25% PEG 8000, 0.2 M sodium tartrate, 0.1 M Mes (pH 6.2)
-
the structure is determined by multiwavelength anomalous diffraction to a resolution of 2.17 A
-
sitting drop method, crystals of native and selenomethionine protein, crystals in complex with dTDP-D-glucose and dTDP-D-xylose
-
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
42
-
E3VXL5
stable for 30 min
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
gene L780, transcription profiling of UGER, phylogenetic analysis
E3VXL5
cloned into pET23b using the Ligation Independent Clone system
-
cloned into pET23a(+) with an N-terminal 6 His tag and a linker consisting of Gly-Ser-Met-Ala, overexpression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
H63A
-
The mutants were examined by circular dichroism, which confirmed no detectable structural changes that would influence the native fold. H63A is catalytically inactive and shows no deuterium incorporation above background at either C3'or C5'.
K73A
-
The mutants were examined by circular dichroism, which confirmed no detectable structural changes that would influence the native fold. K73A is reduced in activity by over 100-fold and a small amount of enzyme catalyzed deuterium incorporation was observed at C5', while only background levels were seen at C3'. This suggests that for the K73A mutant, C5' exchange is more rapid than at C3'.
Y133F
-
The mutants were examined by circular dichroism, which confirmed no detectable structural changes that would influence the native fold. The catalytic activity of the Y133F mutant is reduced 1000-fold but shows some deuterium incorporation at C3' but none at C5' (above background). This indicates that RmlC can catalyze exchange of the proton at C3' without Tyr133 but not at C5'.
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
-
validated anti-bacterial drug target
synthesis
-
the enzyme is part of an enzyme module system for the synthesis of dTDP-activated deoxysugars from dTMP and sucrose
synthesis
-
potential application in altering the enzyme behavior for use in synthesis of bioactive carbohydrates