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Literature summary for 1.2.1.12 extracted from

  • Malhotra, H.; Patidar, A.; Boradia, V.M.; Kumar, R.; Nimbalkar, R.D.; Kumar, A.; Gani, Z.; Kaur, R.; Garg, P.; Raje, M.; Raje, C.I.
    Mycobacterium tuberculosis glyceraldehyde-3-phosphate dehydrogenase (GAPDH) functions as a receptor for human lactoferrin (2017), Front. Cell. Infect. Microbiol., 7, 245 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.2.1.12

Cloned(Commentary)

Cloned (Comment) Organism
gene gap, recombinant expression of His-tagged wild-type and mutant enzymes in Mycobacterium tuberculosis strain H37Ra cell cytosol Mycobacterium tuberculosis

Protein Variants

Protein Variants Comment Organism
N142S naturally occuring mutation, resulting in a non-significant structural change, since Ser at position 142 also shows a similar characteristic to the wild-type residues N142, experimentally the mutation results in a loss of enzyme activity Mycobacterium tuberculosis
P295L naturally occuring mutation Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Mycobacterium tuberculosis 5829
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Mycobacterium tuberculosis
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Mycobacterium tuberculosis H37Rv
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NAD+ Mycobacterium tuberculosis ATCC 25618
-
 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WN83
-
-
Mycobacterium tuberculosis ATCC 25618 P9WN83
-
-
Mycobacterium tuberculosis H37Rv P9WN83
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged wild-type and mutant enzymes from Mycobacterium tuberculosis strain H37Ra cell cytosol by nickel affinity chromatography Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Mycobacterium tuberculosis 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Mycobacterium tuberculosis H37Rv 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?
D-glyceraldehyde 3-phosphate + phosphate + NAD+
-
 Mycobacterium tuberculosis ATCC 25618 3-phospho-D-glyceroyl phosphate + NADH + H+
-
 ?

Subunits

Subunits Comment Organism
homotetramer 4 * 36000, SDS-PAGE Mycobacterium tuberculosis

Synonyms

Synonyms Comment Organism
GAP
-
 Mycobacterium tuberculosis
GAPDH
-
 Mycobacterium tuberculosis
glyceraldehyde-3-phosphate dehydrogenase
-
 Mycobacterium tuberculosis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
 assay at Mycobacterium tuberculosis

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
 Mycobacterium tuberculosis

General Information

General Information Comment Organism
additional information structure homology modeling of GAPDH using the tetrameric GAPDH structure from Bacillus stearothermophilus (PDB ID 1GD1) as template. The glycine-valine-asparagine tripeptide sequence (at positions 140, 141, and 142 respectively) is highly conserved in several GAPDH homologues Mycobacterium tuberculosis
physiological function Mycobacterium tuberculosis relocates several housekeeping proteins to the cell surface for capture and internalization of host iron carrier protein transferrin. One of the identified receptors is the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Mycobacterium tuberculosis glyceraldehyde-3-phosphate dehydrogenase (GAPDH) functions as a receptor for human lactoferrin. Human lactoferrin is sequestered at the bacterial surface by GAPDH. The enzyme is a virulence factor in the bacterium. Iron is chelated by the siderophore and transported via specific iron regulated transporters Mycobacterium tuberculosis