EC Number | Cloned (Comment) | Organism |
---|---|---|
1.2.1.12 | gene gap, recombinant expression of His-tagged wild-type and mutant enzymes in Mycobacterium tuberculosis strain H37Ra cell cytosol | Mycobacterium tuberculosis |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.2.1.12 | 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 |
1.2.1.12 | P295L | naturally occuring mutation | Mycobacterium tuberculosis |
EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|---|
1.2.1.12 | cytosol | - |
Mycobacterium tuberculosis | 5829 | - |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.12 | D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Mycobacterium tuberculosis | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
1.2.1.12 | D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Mycobacterium tuberculosis H37Rv | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
1.2.1.12 | D-glyceraldehyde 3-phosphate + phosphate + NAD+ | Mycobacterium tuberculosis ATCC 25618 | - |
3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.2.1.12 | Mycobacterium tuberculosis | P9WN83 | - |
- |
1.2.1.12 | Mycobacterium tuberculosis ATCC 25618 | P9WN83 | - |
- |
1.2.1.12 | Mycobacterium tuberculosis H37Rv | P9WN83 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.2.1.12 | recombinant His-tagged wild-type and mutant enzymes from Mycobacterium tuberculosis strain H37Ra cell cytosol by nickel affinity chromatography | Mycobacterium tuberculosis |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.2.1.12 | D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Mycobacterium tuberculosis | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
1.2.1.12 | D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Mycobacterium tuberculosis H37Rv | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? | |
1.2.1.12 | D-glyceraldehyde 3-phosphate + phosphate + NAD+ | - |
Mycobacterium tuberculosis ATCC 25618 | 3-phospho-D-glyceroyl phosphate + NADH + H+ | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.2.1.12 | homotetramer | 4 * 36000, SDS-PAGE | Mycobacterium tuberculosis |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.2.1.12 | GAP | - |
Mycobacterium tuberculosis |
1.2.1.12 | GAPDH | - |
Mycobacterium tuberculosis |
1.2.1.12 | glyceraldehyde-3-phosphate dehydrogenase | - |
Mycobacterium tuberculosis |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
1.2.1.12 | 25 | - |
assay at | Mycobacterium tuberculosis |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
1.2.1.12 | 8.5 | - |
assay at | Mycobacterium tuberculosis |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
1.2.1.12 | NAD+ | - |
Mycobacterium tuberculosis |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.2.1.12 | 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 |
1.2.1.12 | 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 |