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Literature summary for 5.1.1.3 extracted from

  • Sengupta, S.; Shah, M.; Nagaraja, V.
    Glutamate racemase from Mycobacterium tuberculosis inhibits DNA gyrase by affecting its DNA-binding (2006), Nucleic Acids Res., 34, 5567-5576.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
Escherichia coli strains DH5a and BL26(DE3) are used for cloning and overexpression of mycobacterial MurI, respectively Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
28800
-
MALDI-TOF analysis Mycobacterium tuberculosis

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
-
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
it is demonstrated that mycobacterial MurI inhibits DNA gyrase activity. Inhibition is not species-specific as Escherichia coli gyrase is also inhibited but is enzyme-specific as topoisomerase I activity remains unaltered. MurI binds to GyrA subunit of the enzyme leading to a decrease in DNA-binding of the holoenzyme. The sequestration of the gyrase by MurI results in inhibition of all reactions catalysed by DNA gyrase. MurI is thus not a typical potent inhibitor of DNA gyrase and instead its role could be in modulation of the gyrase activity Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamate
-
Mycobacterium tuberculosis D-glutamate
-
r

Synonyms

Synonyms Comment Organism
glutamate racemase
-
Mycobacterium tuberculosis
MurI
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Mycobacterium tuberculosis