EC Number |
General Information |
Reference |
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2.8.1.12 | evolution |
homologues of both molybdopterin synthase subunits are evident in diverse eukaryotic sources such as worm, rat, mouse, rice, and fruit fly as well as humans. In contrast, molybdopterin synthase homologues are absent in the yeast Saccharomyces cerevisiae |
722611 |
2.8.1.12 | evolution |
molybdenum cofactor (Moco) biosynthesis is an evolutionarily conserved pathway present in eubacteria, archaea and eukaryotes, including humans. The strong structural similarity between the small subunit of MPT synthase and ubiquitin provides evidence for the evolutionary antecedence of the Moco biosynthetic pathway to the ubiquitin dependent protein degradation pathway |
723255 |
2.8.1.12 | malfunction |
characterization of mutants identified in group B patients of molybdenum cofactor deficiency, molecular mechanism leading to human molybdenum cofactor deficiency, overview |
722634 |
2.8.1.12 | malfunction |
chlorate-sensitive mutants, all the result of amino acid substitutions, produce low levels of molybdopterin and may have low levels of molybdoenzymes. In contrast, chlorate-resistant cnx strains have undetectable levels of molybdopterin, lack the ability to utilize nitrate or hypoxanthine as sole nitrogen sources, and are probably null mutations. Two independent alterations at residue Gly-148 in the large subunit, CnxH, result in temperature sensitivity, not the thermolabile nitrate reductase |
722611 |
2.8.1.12 | malfunction |
chlorate-sensitive mutants, all the result of amino acid substitutions, produce low levels of molybdopterin and may have low levels of molybdoenzymes. In contrast, chlorate-resistant cnx strains have undetectable levels of molybdopterin, lack the ability to utilize nitrate or hypoxanthine as sole nitrogen sources, and are probably null mutations. Two independent alterations at residue Gly-148 in the large subunit, CnxH, result in temperature sensitivity, not the thermolabile nitrate reductase. Molybdopterin is undetectable in the chlorate-resistant mutants, cnxG4 and cnxH3, whereas up to 2% and 10% of the wild-type level is found in the chlorate-sensitive strains cnxG2 and cnxH1, respectively |
722611 |
2.8.1.12 | malfunction |
genetic deficiencies of enzymes involved in Moco biosynthesis in humans lead to a severe and usually fatal disease |
723255 |
2.8.1.12 | malfunction |
the viviparous seed mutant, viviparous15 (vp15), isolated from the Uniform Mu transposon-tagging population, shows an early seedling lethal phenotype, it also shows reduced activities of several enzymes that require molybdenum cofactor (MoCo) in vp15 mutant seedlings, overview. Because MoCo is required for abscisic acid biosynthesis, the viviparous phenotype is probably caused by abscisic acid deficiency |
723418 |
2.8.1.12 | metabolism |
fused MPT synthase protein from Deinococcus radiodurans in which MoaD- and MoaE-like domains are located on a single peptide can be cleaved the JAMM/MPN+ domain containing metalloprotease DR0402 (JAMMDR). Cleavage generates the MoaD having a C-terminal di-Gly motif. JAMMDR can also cleave off the MoaD from MoaD-eGFP fusion protein |
-, 760491 |
2.8.1.12 | metabolism |
molybdopterin (MPT) synthase catalyzes the final step in the biosynthesis of MPT, the metal-binding organic portion of the molybdenum cofactor, Moco |
722628 |
2.8.1.12 | metabolism |
molybdopterin synthase is involved in the conversion of precursor Z to molybdopterin in the molybdenum cofactor biosynthetic pathway |
723281 |