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Information on EC 2.7.7.13 - mannose-1-phosphate guanylyltransferase and Organism(s) Pseudomonas aeruginosa and UniProt Accession P07874

for references in articles please use BRENDA:EC2.7.7.13
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IUBMB Comments
The bacterial enzyme can also use ITP and dGTP as donors.
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Select one or more organisms in this record:
This record set is specific for:
Pseudomonas aeruginosa
UNIPROT: P07874
Word Map
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The taxonomic range for the selected organisms is: Pseudomonas aeruginosa
Synonyms
BceA, BceA(J) protein, BceAJ, GDP-alpha-D-mannose pyrophosphorylase, GDP-D-mannose pyrophosphorylase, GDP-Man pyrophosphorylase, GDP-mannose pyrophosphorylase, GDP-mannose pyrophosphorylase B, GDP-ManPP, GDP-MP, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GDP-mannose pyrophosphorylase
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GTP-mannose 1-phosphate guanylyltransferase
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GTP-mannose-1-phosphate guanylyltransferase
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guanosine 5'-diphospho-D-mannose pyrophosphorylase
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guanosine diphosphomannose pyrophosphorylase
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guanosine triphosphate-mannose 1-phosphate guanylyltransferase
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guanylyltransferase, mannose 1-phosphate
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mannose 1-phosphate guanylyltransferase (guanosine triphosphate)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
GTP + alpha-D-mannose 1-phosphate = diphosphate + GDP-mannose
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nucleotidyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
GTP:alpha-D-mannose-1-phosphate guanylyltransferase
The bacterial enzyme can also use ITP and dGTP as donors.
CAS REGISTRY NUMBER
COMMENTARY hide
37278-24-3
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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
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
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
GTP + alpha-D-mannose 1-phosphate
GDPmannose + diphosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
Mg2+ or Mn2+ required for activity
Mn2+
Mg2+ or Mn2+ required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0205
D-mannose 1-phosphate
pH 8.0, 25°C
0.0142
GDPmannose
pH 7.0, 25°C
0.0295 - 0.041
GTP
0.0082
mannose 1-phosphate
25°C, cosubstrate GTP
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
54000
gel filtration, phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase is a bifunctional enzyme catalyzing both the phosphomannose isomerase, i.e. PIM, and guanosine 5'-diphospho-D-mannose pyrophosphorylase, i.e. GMP, reaction
56000
1 * 56000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 56000, SDS-PAGE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
K175E
approx. 9% of wild-type activity, 600fold increase in Km for mannose 1-phosphate
K175Q
approx. 40% of wild-type activity, 3200fold increase in Km for mannose 1-phosphate
K175R
470fold increase in mannose 1-phosphate Km value
K20Q
enzyme is unable to support alginate synthesis although it shows no significant differences in Vmax and Km as compared to wild-type
R19H
approx. 50% of wild-type activity, 8fold increase in Km for mannose 1-phosphate
R19K
approx. 50% of wild-type activity, 2 and 6fold increase in Km for mannose 1-phosphate and GTP, respectively
R19L
approx. 50% of wild-type activity, 5fold increase in Km for mannose 1-phosphate and GTP, respectively
S12A
approx. 44% of wild-type activity, 2 and 3fold decrease in Km for mannose 1-phosphate and GTP, respectively
PURIFICATION/commentary
ORGANISM
UNIPROT
LITERATURE
Biogel, Q-Sepharose, Sephacryl-200
CLONED/commentary
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and several PMI-GMP mutants in algA mutant 8853
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
May, T.B.; Shinabarger, D.; Boyd, A.; Chakrabarty, A.M.
Identification of amino acid residues involved in the activity of phosphomannose isomerase-guanosine 5'-diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa
J. Biol. Chem.
269
4872-4877
1994
Pseudomonas aeruginosa (P07874)
Manually annotated by BRENDA team
Shinabarger, D.; Berry, A.; May, T.B.; Rothmel, R.; Fialho, A.; Chakrabarty, A.M.
Purification and characterization of phosphomannose isomerase-guanosine diphospho-D-mannose pyrophosphorylase. A bifunctional enzyme in the alginate biosynthetic pathway of Pseudomonas aeruginosa
J. Biol. Chem.
266
2080-2088
1991
Pseudomonas aeruginosa (P07874), Pseudomonas aeruginosa
Manually annotated by BRENDA team
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