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Literature summary for 2.3.1.1 extracted from

  • Errey, J.C.; Blanchard, J.S.
    Functional characterization of a novel ArgA from Mycobacterium tuberculosis (2005), J. Bacteriol., 187, 3039-3044.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.3.1.1

Cloned(Commentary)

Cloned (Comment) Organism
gene Rv2747 or argA, expression of the His-tagged enzyme in Escherichia coli Mycobacterium tuberculosis

Inhibitors

Inhibitors Comment Organism Structure
acetyl-CoA substrate inhibition Mycobacterium tuberculosis
L-arginine feedback inhibition, regulatory function, 50% inhibition at 0.026 mM, complete inhibition at 0.5 mM, negatively cooperative binding Mycobacterium tuberculosis
L-glutamine substrate inhibition Mycobacterium tuberculosis
additional information no inhibition by other proteinogenic L-amino acids Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information no saturation with L-glutamate up to 600 mM Mycobacterium tuberculosis
0.15
-
 acetyl-CoA
-
 Mycobacterium tuberculosis
280
-
 L-glutamine
-
 Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
-
 Mycobacterium tuberculosis
20978
-
 2 * 21000, SDS-PAGE, 2 * 20978, mass spectrometry Mycobacterium tuberculosis
20978
-
 4 * 21000, SDS-PAGE, 4 * 20978, mass spectrometry Mycobacterium tuberculosis
21000
-
 2 * 21000, SDS-PAGE, 2 * 20978, mass spectrometry Mycobacterium tuberculosis
21000
-
 4 * 21000, SDS-PAGE, 4 * 20978, mass spectrometry Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
acetyl-CoA + L-glutamate Mycobacterium tuberculosis initial step of the L-arginine biosynthesis, pathway overview CoA + N-acetyl-L-glutamate
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
 gene Rv2747 or argA
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography, ammonium sulfate fractionation, gel filtration, and ultrafiltration Mycobacterium tuberculosis

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + L-glutamate = CoA + N-acetyl-L-glutamate sequential kinetic mechanism Mycobacterium tuberculosis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + L-glutamate
-
 Mycobacterium tuberculosis CoA + N-acetyl-L-glutamate
-
 ?
acetyl-CoA + L-glutamate initial step of the L-arginine biosynthesis, pathway overview Mycobacterium tuberculosis CoA + N-acetyl-L-glutamate
-
 ?
acetyl-CoA + L-glutamine
-
 Mycobacterium tuberculosis CoA + N-acetyl-L-glutamine
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 21000, SDS-PAGE, 2 * 20978, mass spectrometry Mycobacterium tuberculosis
More the enzyme exists at equal amounts as dimer and tetramer, the monomer consists of 2 domains with the catalytic active site being located at the C-terminal domain Mycobacterium tuberculosis
tetramer 4 * 21000, SDS-PAGE, 4 * 20978, mass spectrometry Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
ArgA
-
 Mycobacterium tuberculosis
More the enzyme is a member of the GCN5-related N-acetyltransferase superfamily Mycobacterium tuberculosis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.22
-
 L-glutamate
-
 Mycobacterium tuberculosis
0.78
-
 L-glutamine
-
 Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
acetyl-CoA
-
 Mycobacterium tuberculosis

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.015
-
 acetyl-CoA
-
 Mycobacterium tuberculosis
30
-
 L-glutamine
-
 Mycobacterium tuberculosis