Information on EC 4.2.1.159 - dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-dehydratase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
4.2.1.159
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RECOMMENDED NAME
GeneOntology No.
dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-dehydratase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dTDP-(2R,6S)-2,4-dihydroxy-6-methyl-2,6-dihydropyran-3-one = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose
show the reaction diagram
(1b), spontaneous
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dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose = dTDP-(2R,6S)-2,4-dihydroxy-6-methyl-2,6-dihydropyran-3-one + H2O
show the reaction diagram
(1a)
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dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H2O
show the reaction diagram
overall reaction
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Biosynthesis of antibiotics
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Biosynthesis of vancomycin group antibiotics
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Polyketide sugar unit biosynthesis
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dTDPLrhamnose biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose hydro-lyase (dTDP-(2R,6S)-2,4-dihydroxy-6-methyl-2,6-dihydropyran-3-one-forming)
The enzyme participates in the biosynthesis of several deoxysugars, including beta-L-4-epi-vancosamine, alpha-L-megosamine, L- and D-olivose, D-oliose, D-mycarose, forosamine and beta-L-digitoxose. In vitro the intermediate can undergo a spontaneous decomposition to maltol [2,3].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
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-alpha-D-glucopyranose
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H2O
show the reaction diagram
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-4-dehydro-6-deoxy-alpha-D-glucopyranose
dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H2O
show the reaction diagram
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enzyme MegBVI is involved in the C-2 deoxygenation step during the biosynthesis of TDP-L-mycarose, generating the intermediate TDP-2,6-dideoxy-3,4-dioxo-D-glucose
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?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.038 - 0.056
dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
to 1.7 A resolution. Each subunit of the EvaA dimer folds into two domains that clearly arose via gene duplication. Two dTDP-sugar binding pockets, A and B, are present in each EvaA subunit. Pocket A functions as the active site and pocket B is simply a remnant left behind from the gene duplication event
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E139Q
complete loss of catalytic activity
E190A
complete loss of catalytic activity
E190Q
complete loss of catalytic activity
E231A/E233A
mutant constructed to reduce surface entropy. None of the resulting crystals demonstrates improved diffraction properties
E316A/K317A
mutant constructed to reduce surface entropy. None of the resulting crystals demonstrates improved diffraction properties
E405
complete loss of catalytic activity
E405A
complete loss of catalytic activity
K289A/Q290A/E293A
mutant constructed to reduce surface entropy. None of the resulting crystals demonstrates improved diffraction properties
R381A
mutant with improved crystallization parameters, kinetic parameters similar to wild-type
E139Q
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complete loss of catalytic activity
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E190A
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complete loss of catalytic activity
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E190Q
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complete loss of catalytic activity
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E405A
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complete loss of catalytic activity
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R381A
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mutant with improved crystallization parameters, kinetic parameters similar to wild-type
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
construction of a Streptomyces albus strain harboring the oleG2 glycosyltransferase gene and transformation with plasmid constructs containing a set of genes proposed to be required for the biosynthesis of dTDP-L-olivose and dTDP-L-oleandrose, respectively. Incubation of these strains with the erythromycin aglycon (erythronolide B) gives rise to two new glycosylated compounds, identified as L-3-O-olivosyl- and L-3-O-oleandrosyl-erythronolide B. Plasmid constructs pOLV and pOLE containing the oleW, oleV, oleL, oleS, oleE, and oleU genes and the 5' end of oleNI encode all enzyme activities required for the biosynthesis of these two 2,6-dideoxysugars