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Literature summary for 1.2.1.12 extracted from

  • Bergmann, S.; Rohde, M.; Hammerschmidt, S.
    Glyceraldehyde-3-phosphate dehydrogenase of Streptococcus pneumoniae is a surface-displayed plasminogen-binding protein (2004), Infect. Immun., 72, 2416-2419.
    View publication on PubMedView publication on EuropePMC

Localization

Localization Comment Organism GeneOntology No. Textmining
cell surface
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Streptococcus pneumoniae 9986
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cytoplasm
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Streptococcus pneumoniae 5737
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Streptococcus pneumoniae the concerted action of both alpha-enolase and GAPDH on the bacterial cell surface might result in an enhancement of the pathogen‘s ability to degrade the extracellular matrix and to invade host tissues ?
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?

Organism

Organism UniProt Comment Textmining
Streptococcus pneumoniae I6L8L9
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-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the concerted action of both alpha-enolase and GAPDH on the bacterial cell surface might result in an enhancement of the pathogen‘s ability to degrade the extracellular matrix and to invade host tissues Streptococcus pneumoniae ?
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?
additional information the enzyme has a specific plasmin- and plasminogen-binding activity, high affinity for plasmin and significantly lower affinity for plasminogen Streptococcus pneumoniae ?
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?