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Literature summary for 1.4.1.10 extracted from

  • Giffin, M.M.; Modesti, L.; Raab, R.W.; Wayne, L.G.; Sohaskey, C.D.
    ald of Mycobacterium tuberculosis encodes both the alanine dehydrogenase and the putative glycine dehydrogenase (2012), J. Bacteriol., 194, 1045-1054.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
gene ald, quantitative real-time PCR expression analysis, expression in Escherichia coli strain ER2566 Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
additional information generation of ald knockout strain RVW7 from wild-type strain H37Rv Mycobacterium tuberculosis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.5
-
glyoxylate pH 8.5, 22°C, recombinant enzyme Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol minor fraction Mycobacterium tuberculosis 5829
-
membrane major fraction Mycobacterium tuberculosis 16020
-
additional information no enzyme detected in the extracellular medium Mycobacterium tuberculosis
-
-

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis
-
gene ald
-
Mycobacterium tuberculosis H37Rv
-
gene ald
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged enzyme from Escherichia coli strain ER2566 by nickel affinity chromatography, native enzyme by anion exchange and hydrophobic interaction chromatography, followed by ultrafiltration Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glyoxylate + NH3 + NADH + H+
-
Mycobacterium tuberculosis glycine + H2O + NAD+
-
ir
glyoxylate + NH3 + NADH + H+
-
Mycobacterium tuberculosis H37Rv glycine + H2O + NAD+
-
ir
additional information the putative glycine dehydrogenase of Mycobacterium tuberculosis catalyzes the reductive amination of glyoxylate to glycine but not the reverse reaction. It exhbits both pyruvate and glyoxylate aminating activitiesand also shows alanine dehydrogenase activity, EC 1.4.1.1, to a greater extent than glyoxylate aminating activity Mycobacterium tuberculosis ?
-
?
additional information the putative glycine dehydrogenase of Mycobacterium tuberculosis catalyzes the reductive amination of glyoxylate to glycine but not the reverse reaction. It exhbits both pyruvate and glyoxylate aminating activitiesand also shows alanine dehydrogenase activity, EC 1.4.1.1, to a greater extent than glyoxylate aminating activity Mycobacterium tuberculosis H37Rv ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Mycobacterium tuberculosis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
NADH
-
Mycobacterium tuberculosis

Expression

Organism Comment Expression
Mycobacterium tuberculosis transcription of ald is induced when alanine is the sole nitrogen source up

General Information

General Information Comment Organism
physiological function the enzyme plays an essential role in the utilization of alanine, but not of glycine, as a nitrogen source Mycobacterium tuberculosis