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Literature summary for 4.1.2.13 extracted from

  • Tunio, S.A.; Oldfield, N.J.; Berry, A.; Alaaldeen, D.A.; Wooldridge, K.G.; Turner, D.P.
    The moonlighting protein fructose-1, 6-bisphosphate aldolase of Neisseria meningitidis: surface localization and role in host cell adhesion (2010), Mol. Microbiol., 76, 605-615.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
TOP10F' and BL21(DE3) pLysS are used for the expression of 6x histidine-tagged recombinant enzyme encoded by plasmid pSAT-FBA Neisseria meningitidis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.05
-
D-fructose 1,6-bisphosphate at 30°C in 50 mM Tris-HCl, 0.1 M potassium acetate buffer (pH 8.0) Neisseria meningitidis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
Neisseria meningitidis 5737
-
outer membrane
-
Neisseria meningitidis 19867
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
38000
-
SDS-PAGE Neisseria meningitidis

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
HisPur cobalt resin column chromatography Neisseria meningitidis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-fructose 1,6-bisphosphate
-
Neisseria meningitidis glycerone phosphate + D-glyceraldehyde 3-phosphate
-
?

Synonyms

Synonyms Comment Organism
FBA
-
Neisseria meningitidis
fructose-1,6-bisphosphate aldolase
-
Neisseria meningitidis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.1
-
D-fructose 1,6-bisphosphate at 30°C in 50 mM Tris-HCl, 0.1 M potassium acetate buffer (pH 8.0) Neisseria meningitidis

General Information

General Information Comment Organism
physiological function FBA is required for optimal adhesion of meningococci to human cells Neisseria meningitidis