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Literature summary for 4.1.2.13 extracted from

  • Shams, F.; Oldfield, N.J.; Lai, S.K.; Tunio, S.A.; Wooldridge, K.G.; Turner, D.P.
    Fructose-1,6-bisphosphate aldolase of Neisseria meningitidis binds human plasminogen via its C-terminal lysine residue (2016), MicrobiologyOpen, 5, 340-350 .
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
-
Neisseria meningitidis
expressed in Escherichia coli JM109 cells Neisseria meningitidis

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
-
Neisseria meningitidis 9986
-
cell surface surface-exposed enzyme Neisseria meningitidis 9986
-

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Neisseria meningitidis
Ni Sepharose 6 column chromatography and Sephadex G-25 gel filtration 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
-
?
additional information the enzyme binds to human glu-plasminogen in a dose-dependent manner Neisseria meningitidis ?
-
?

Synonyms

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

General Information

General Information Comment Organism
physiological function the enzyme is involved in adhesion to host cells. It binds human plasminogen via its C-terminal lysine residue, whereas subterminal lysine residues are not involved Neisseria meningitidis