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Literature summary for 2.7.7.80 extracted from
- Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor (2001), J. Biol. Chem., 276, 34695-34701.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene moeB, DNA and amino acid sequence determinations, expression of wild-type MoeB in Escherichia coli strain BL21(DE3) and of MoeB mutants in Escerichia coli strain moeB- (DE3) cells from pMW15eB | Escherichia coli |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| C128A | site-directed mutagenesis, completely active mutant | Escherichia coli |
| C128Y | site-directed mutagenesis, completely active mutant | Escherichia coli |
| C142A | site-directed mutagenesis, the mutant shows activity like the wild-type enzyme | Escherichia coli |
| C142A/C187A | site-directed mutagenesis, the mutant shows activity like the wild-type enzyme | Escherichia coli |
| C172A | site-directed mutagenesis, the mutant's Zn2+ content is below the limit of detection, the activity is reduced compared to the wild-type enzyme | Escherichia coli |
| C175A | site-directed mutagenesis, the mutant's Zn2+ content is below the limit of detection, the activity is reduced compared to the wild-type enzyme | Escherichia coli |
| C187A | site-directed mutagenesis, the mutant shows activity like the wild-type enzyme | Escherichia coli |
| C231A | site-directed mutagenesis, the mutant shows activity like the wild-type enzyme | Escherichia coli |
| C244A | site-directed mutagenesis, the mutant's Zn2+ content is below the limit of detection, the activity is reduced compared to the wild-type enzyme | Escherichia coli |
| C247A | site-directed mutagenesis, the mutant's Zn2+ content is below the limit of detection, the activity is reduced compared to the wild-type enzyme | Escherichia coli |
| C44A | site-directed mutagenesis, the mutant shows activity like the wild-type enzyme | Escherichia coli |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | required | Escherichia coli |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 52000 | - |
x * 52000, recombinant enzyme, SDS-PAGE | Escherichia coli |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly | Escherichia coli | - |
diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Escherichia coli | P12282 | gene moeB | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant wild-type and mutant MoeBs from Escherichia coli strain BL21(DE3) by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration | Escherichia coli |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| ATP + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly | - |
Escherichia coli | diphosphate + [molybdopterin-synthase sulfur-carrier protein]-Gly-Gly-AMP | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 52000, recombinant enzyme, SDS-PAGE | Escherichia coli |
| More | two CXXC motifs near the C-terminus of MoeB. The MoeB-MoaD adenylate complex is a tetramer with a mass of 71.8 kDa | Escherichia coli |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| MoeB | - |
Escherichia coli |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 22 | - |
assay at room temperature | Escherichia coli |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 7.5 | - |
assay at | Escherichia coli |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | The Escherichia coli moeB mutant strains contain an inactive, desulfo form of MPT synthase. Substitutions of every cysteine residue in MoeB does not affect activity, except for the mutations in the cysteine residues located in putative Zn-binding motifs, which cause loss of metal binding correlated with loss of activity | Escherichia coli |
| physiological function | MoeB is involved in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor. MoeB-dependent formation of a C-terminal thiocarboxylate on the MoaD subunit of molybdopterin synthase might resemble the ubiquitin-activating step in the ubiquitin-targeted degradation of proteins in eukaryotes, but without formation of a thioester intermediate between MoeB and MoaD, overview. But formation of a complex of MoeB and MoaD adenylate, that is stable to gel filtration, occurs | Escherichia coli |
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