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Information on EC 2.7.7.24 - glucose-1-phosphate thymidylyltransferase and Organism(s) Pseudomonas aeruginosa and UniProt Accession Q9HU22

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IUBMB Comments
Involved in the biosynthesis of L-rhamnose in bacteria.
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This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: Q9HU22
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The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
The enzyme appears in selected viruses and cellular organisms
Synonyms
glucose-1-phosphate thymidylyltransferase, cps2l, dtdp-glucose synthase, sgca1, glc-1-p-tt, sugar-1-phosphate nucleotidyltransferase, dtdp-d-glucose synthase, d-glucose-1-phosphate thymidylyltransferase, dtdpglucose pyrophosphorylase, dtdp-glucose-pyrophosphorylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dTDP-glucose synthase
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dTDP-glucose-pyrophosphorylase
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dTDPglucose pyrophosphorylase
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glucose 1-phosphate thymidylyltransferase
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glucose-1-phosphate thymidylyltransferase
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TDP-glucose pyrophosphorylase
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thymidine diphosphate glucose pyrophosphorylase
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thymidine diphosphoglucose pyrophosphorylase
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thymidylyltransferase, glucose 1-phosphate
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-
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
dTTP + alpha-D-glucose 1-phosphate = diphosphate + dTDP-alpha-D-glucose
show the reaction diagram
ordered bi-bi mechanism
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
dTTP:alpha-D-glucose-1-phosphate thymidylyltransferase
Involved in the biosynthesis of L-rhamnose in bacteria.
CAS REGISTRY NUMBER
COMMENTARY hide
9026-03-3
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
dTTP + alpha-D-glucose 1-phosphate
dTDP-glucose + diphosphate
show the reaction diagram
TTP + alpha-D-glucose 1-phosphate
TDP-glucose + diphosphate
show the reaction diagram
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-
-
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r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
dTTP + alpha-D-glucose 1-phosphate
dTDP-glucose + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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absolute requirement, 2 mM: optimal
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-(6-amino-1-benzyl-1,2,3,4-tetrahydropyrimidin-5-yl)-N-methylbenzenesulfonamide
inhibitor does not bind at the active site of RmlA but binds at a second site remote from the active site. Despite this, the compound acts as competitive inhibitor but with high cooperativity
N-(6-amino-1-benzyl-1,2,3,4-tetrahydropyrimidin-5-yl)-N-methylbutane-1-sulfonamide
inhibitor does not bind at the active site of RmlA but binds at a second site remote from the active site. Despite this, the compound acts as competitive inhibitor but with high cooperativity
N-(6-amino-1-benzyl-1,2,3,4-tetrahydropyrimidin-5-yl)-N-methylfuran-2-sulfonamide
inhibitor does not bind at the active site of RmlA but binds at a second site remote from the active site. Despite this, the compound acts as competitive inhibitor but with high cooperativity
dTDP-L-rhamnose
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.05
TDP-glucose
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25°C, pH 8
0.1
TTP
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25°C, pH 8
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.000073
N-(6-amino-1-benzyl-1,2,3,4-tetrahydropyrimidin-5-yl)-N-methylbenzenesulfonamide
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
0.000175
N-(6-amino-1-benzyl-1,2,3,4-tetrahydropyrimidin-5-yl)-N-methylbutane-1-sulfonamide
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
0.000105
N-(6-amino-1-benzyl-1,2,3,4-tetrahydropyrimidin-5-yl)-N-methylfuran-2-sulfonamide
Pseudomonas aeruginosa
pH not specified in the publication, temperature not specified in the publication
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44.8
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dTDPglucose + diphosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
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assay at, dTDP-glucose + diphosphate
37
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assay at, dTTP + alpha-D-glucose 1-phosphate
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
106000 - 122000
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dynamic light scattering
33770
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calculated from nucleic acid sequence
33800
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MALDI mass spectrum
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
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each monomer consisting of three functional subunits
additional information
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trimer or tetramer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting-drop vapour-diffusion method in polyethylene glycol 6000, 0.1 M sodium citrate, pH 4.6 and 0.5 M Li2SO4 as precipitant, crystallization as apoenzyme or co-crystallization with dTTP or thymidine and alpha-D-glucose 1-phosphate or dTDP-D-glucose or dTDP-L-rhamnose
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sitting-drop vapour-diffusion method in polyethylene glycol 6000, 0.1 M sodium citrate, pH 4.6 and 0.5 M Li2SO4 as precipitant, space group: P1, the asymmetric unit contains eight monomers in the form of two RmlA tetramers with a solvent content of 51%
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sitting-drop vapour-diffusion technique with PEG 6000 and lithium sulfate as precipitant. Several diffraction data sets of single frozen crystals are collected to a resolution of 1.66 A. Crystals belong to space group P1, with unit-cell parameters a = 71.5 A, b = 73.1 A, c = 134.7 A, alpha = 89.9°, beta = 80.9°, gamma = 81°
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
stable for several weeks at any step of purification if kept frozen
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ATCC 7700, partial
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recombinant enzyme with his-tag
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli BL21 with a 6 x His-tag
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kornfeld, S.; Glaser, L.
The enzymatic synthesis of thymidine-linked sugars I. Thymidine diphosphate glucose
J. Biol. Chem.
236
1791-1794
1961
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Blankenfeldt, W.; Giraud, M.F.; Leonard, G.; Rahim, R.; Creuzenet, C.; Lam, J.S.; Naismith, J.H.
The purification, crystallization and preliminary structural characterization of glucose-1-phosphate thymidylyltransferase (RmlA), the first enzyme of the dTDP-L-rhamnose synthesis pathway from Pseudomonas aeruginosa
Acta Crystallogr. Sect. D
56
1501-1504
2000
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Blankenfeldt, W.; Asuncion, M.; Lam, J.S.; Naismith, J.H.
The structural basis of the catalytic mechanism and regulation of glucose-1-phosphate thymidylyltransferase (RmlA)
EMBO J.
19
6652-6663
2000
Pseudomonas aeruginosa
Manually annotated by BRENDA team
Alphey, M.S.; Pirrie, L.; Torrie, L.S.; Boulkeroua, W.A.; Gardiner, M.; Sarkar, A.; Maringer, M.; Oehlmann, W.; Brenk, R.; Scherman, M.S.; McNeil, M.; Rejzek, M.; Field, R.A.; Singh, M.; Gray, D.; Westwood, N.J.; Naismith, J.H.
Allosteric competitive inhibitors of the glucose-1-phosphate thymidylyltransferase (RmlA) from Pseudomonas aeruginosa
ACS Chem. Biol.
8
387-396
2013
Pseudomonas aeruginosa (Q9HU22), Pseudomonas aeruginosa
Manually annotated by BRENDA team