EC Number   |
General Information |
Reference |
|---|
    2.1.2.1 | evolution |
serine hydroxymethyltransferase is a ubiquitous representative of the family of fold type I pyridoxal 5'-phosphate-dependent enzymes, structural determinants, overview |
718984 |
| 2.1.2.1 | evolution |
SHMT is a ubiquitous enzyme and its sequence and structure were conserved during divergent evolution. SHMT belongs to the fold type-I superfamily of PLP-dependent enzymes, a very complex group of proteins arising from an intricate evolutionary process |
-, 737188 |
| 2.1.2.1 | evolution |
the enzyme belongs to the alpha class of PLP-dependent enzymes. The ligand binding environment of enzymes SHMT from human and Plasmodium are different, overview |
736084 |
| 2.1.2.1 | evolution |
the enzyme belongs to the alpha-family of fold type I, and pyridoxal 5'-phosphate-dependent enzymes |
-, 735436 |
| 2.1.2.1 | evolution |
the enzyme belongs to the fold type-I superfamily of PLP-dependent enzymes |
737212 |
| 2.1.2.1 | malfunction |
a shm1 null mutant requires CO2-enriched air to inhibit photorespiration, while a shm2 null mutant does not show any visible impairment, a double-null mutant cannot survive in CO2-enriched air. Residual SHM activity is undetectably low in purified leaf mesophyll mitochondria of the shm1 mutant. In roots, the knockout of SHM1 does not reduce total SHM activity, whereas the knockout of SHM2 significantly lowers total SHM activity |
720740 |
| 2.1.2.1 | malfunction |
a shm1mutant has chlorotic lesions and a considerably smaller, lethal phenotype under natural ambient CO2 concentrations, but can be restored to wild type with normal growth under elevated CO2 levels (0.5% CO2), showing a typical photorespiratory phenotype |
757362 |
| 2.1.2.1 | malfunction |
digestion of blood is inhibited in enzyme RNAi-silenced female Aedes aegypti mosquitoes. Enzyme-depleted female mosquitoes lose their flight ability and die within 48 h of a blood meal |
-, 757905 |
| 2.1.2.1 | malfunction |
overexpression of mitochondrial serine hydroxymethyltransferase assures an adequate supply of glycine to rapidly proliferating cancer cells, silencing of mitochondrial serine hydroxymethyltransferase halts cancer cell proliferation and supplementation with sarcosine (a glycine-related metabolite) or formate (a source of one carbon units) fails to rescue cell proliferation |
736727 |
| 2.1.2.1 | malfunction |
Shmt1 null mice are fertile and do not demonstrate maternal lethality |
704435 |
