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Literature summary for 1.11.1.25 extracted from

  • Aljannat, M.; Oldfield, N.; Albasri, H.; Dorrington, L.; Ohri, R.; Wooldridge, K.; Turner, D.
    The moonlighting peroxiredoxin-glutaredoxin in Neisseria meningitidis binds plasminogen via a C-terminal lysine residue and contributes to survival in a whole blood model (2020), Microb. Pathog., 139, 103890 .
    View publication on PubMed
Search for more literature for 1.11.1.25

Cloned(Commentary)

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

Protein Variants

Protein Variants Comment Organism
C185A active site mutant Neisseria meningitidis
C185A the mutant shows improved binding to plasminogen Neisseria meningitidis
K230A the mutant shows impaired binding to plasminogen Neisseria meningitidis
K230A/K244A the mutant shows impaired binding to plasminogen Neisseria meningitidis
K244A the mutant shows slightly impaired binding to plasminogen Neisseria meningitidis

Inhibitors

Inhibitors Comment Organism Structure
epsilon-aminocapronic acid
-
 Neisseria meningitidis

Localization

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

Organism

Organism UniProt Comment Textmining
Neisseria meningitidis Q7DDK4
-
-
Neisseria meningitidis MC58 Q7DDK4
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni Sepharose column chromatography and Sephadex G-25 gel filtration Neisseria meningitidis

Source Tissue

Source Tissue Comment Organism Textmining

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information Prx5-Grx is a plasminogen-binding protein Neisseria meningitidis ?
-
-
additional information Prx5-Grx is a plasminogen-binding protein Neisseria meningitidis MC58 ?
-
-

Synonyms

Synonyms Comment Organism
peroxiredoxin-glutaredoxin
-
 Neisseria meningitidis
Prx5-Grx
-
 Neisseria meningitidis

General Information

General Information Comment Organism
malfunction the enzyme-deficient mutant has a survival defect in human whole blood compared with the parental or complemented strain Neisseria meningitidis
physiological function the enzyme plays an important role in meningococcal pathogenesis and enhances meningococcal survival under oxidative stress Neisseria meningitidis