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Literature summary for 2.8.1.12 extracted from
- Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation (2001), Nat. Struct. Biol., 8, 42-46.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| recombinant expression in Escherichia coli strain BL21(DE3) | Homo sapiens |
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| purified recombinant enzyme, vapor diffusion, protein in M NaCl, 0.1 M HEPES, pH 7.5, is mixed with mother liquor containing 20% v/v glycerol, X-ray diffraction structure determination and analysis at 1.45 A resolution | Homo sapiens |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | O96007 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant enzyme from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, dialysis, and gel filtration | Homo sapiens |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| heterotetramer | the crystal structure of MPT synthase reveals a heterotetrameric protein in which the C-terminus of each small subunit is inserted into a large subunit to form the active site | Homo sapiens |
| More | comparison of structures and sequences of MPT synthases from different species, overview. The side chains of the aromatic residues Phe D7, Phe D75, Tyr E55 and Trp E125 are forming the hydrophobic core of the heterodimer interface, the highly conserved active site residues are Arg39, Lys119, Lys126 and Arg140 in the large subunit | Homo sapiens |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MPT synthase | - |
Homo sapiens |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | - |
assay at | Homo sapiens |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8 | - |
assay at | Homo sapiens |
General Information
| General Information | Comment | Organism |
|---|---|---|
| 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 | Homo sapiens |
| malfunction | genetic deficiencies of enzymes involved in Moco biosynthesis in humans lead to a severe and usually fatal disease | Homo sapiens |
| additional information | in the activated form of the enzyme this C-terminus is present as a thiocarboxylate. In the structure of a covalent complex of MPT synthase, an isopeptide bond is present between the C-terminus of the small subunit and a Lys side chain in the large subunit. The highly conserved active site residues are Arg39, Lys119, Lys126 and Arg140 in the large subunit | Homo sapiens |
| physiological function | the molybdenum cofactor contains a tricyclic pyranopterin, termed molybdopterin (MPT), that bears the cis-dithiolene group responsible for molybdenum ligation. The dithiolene group of MPT is generated by MPT synthase | Homo sapiens |
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