Application | Comment | Organism |
---|---|---|
analysis | radiochemical assay for the bifunctional enzyme that monitors the formation of acid stable [14C]-DTB from acid-labile 14CO2 in the presence of appropriate substrates and cofactors | Arabidopsis thaliana |
Cloned (Comment) | Organism |
---|---|
- |
Arabidopsis thaliana |
expression in Escherichia coli as truncated protein, with an N-terminal 22-residue deletion | Arabidopsis thaliana |
Crystallization (Comment) | Organism |
---|---|
crystallization of the native and the selenomethionine enzyme, without ligand in two different space groups. In both cases, the structures show a dimer made of two monomers related by a noncrystallographic twofold axis | Arabidopsis thaliana |
native and the selenomethionine enzyme without ligand, in two different space groups. The structures show a dimer made of two monomers related by a noncrystallographic twofold axis | Arabidopsis thaliana |
Protein Variants | Comment | Organism |
---|---|---|
F326Y | no major impact on kinetic parameters | Arabidopsis thaliana |
F326Y | mutant improves the recombinant enzyme solubility and stability | Arabidopsis thaliana |
I793W | mutation predicted to obstruct the observed external crevice. In contrast with the wild-type enzyme, mutant exhibits progress curves with an obvious lag phase with extrapolated transient times of 12 min, as expected for nonchanneling controls | Arabidopsis thaliana |
I793W | mutant is predicted to obstruct the observed external crevice. Mutant exhibits progress curves with obvious lag phases with extrapolated transient times of 10 to 12 min, as expected for nonchanneling controls | Arabidopsis thaliana |
S360Y | mutation predicted to obstruct the observed external crevice. In contrast with the wild-type enzyme, mutant exhibits progress curves with an obvious lag phase with extrapolated transient times of 10 min, as expected for nonchanneling controls | Arabidopsis thaliana |
S360Y | mutant is predicted to obstruct the observed external crevice. Mutant exhibits progress curves with obvious lag phases with extrapolated transient times of 10 to 12 min, as expected for nonchanneling controls | Arabidopsis thaliana |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.0046 | - |
8-Amino-7-oxononanoate | mutant F326Y, pH 8.6, 37°C | Arabidopsis thaliana | |
0.0046 | - |
8-Amino-7-oxononanoate | mutant F326Y, K0.5 value, Hill coefficient 1.36, pH 8.6, 37°C | Arabidopsis thaliana | |
0.0048 | - |
8-Amino-7-oxononanoate | wild-type, pH 8.6, 37°C | Arabidopsis thaliana | |
0.0048 | - |
8-Amino-7-oxononanoate | wild-type, K0.5 value, Hill coefficient 1.29, pH 8.6, 37°C | Arabidopsis thaliana | |
0.6 | 3 | S-adenosyl-L-methionine | wild-type, K0.5 value, Hill coefficient 1.34, pH 8.6, 37°C | Arabidopsis thaliana | |
0.63 | - |
S-adenosyl-L-methionine | wild-type, pH 8.6, 37°C | Arabidopsis thaliana | |
1.63 | - |
S-adenosyl-L-methionine | mutant F326Y, pH 8.6, 37°C | Arabidopsis thaliana | |
1.65 | - |
S-adenosyl-L-methionine | mutant F326Y, K0.5 value, Hill coefficient 1.23, pH 8.6, 37°C | Arabidopsis thaliana |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
mitochondrion | - |
Arabidopsis thaliana | 5739 | - |
mitochondrion | mitochondrial matrix | Arabidopsis thaliana | 5739 | - |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
90000 | - |
x * 90000, SDS-PAGE | Arabidopsis thaliana |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Arabidopsis thaliana | the BIO3-BIO1 fusion protein is the sole protein form produced by the BIO3-BIO1 locus in Arabidopsis. The enzyme catalyzes both diaminopelargonic acid aminotransferase and dethiobiotin synthetase reactions in vitro. In the course of the reaction, the diaminopelargonic acid intermediate is directly transferred from the both diaminopelargonic acid aminotransferase active site to the dethiobiotin synthetase active site | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | B0F481 | bifunctional dethiobiotin synthetase/diaminopelargonic acid aminotransferase | - |
Arabidopsis thaliana | B0F481 | bifunctional enzyme dethiobiotin synthetase-diaminopelargonic acid aminotransferase, gene produces a bicistronic transcript potentially encoding separate monofunctional proteins that can be produced following an alternative splicing mechanism | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | no substrates: L-Asp, L-Glu, L-Met, L-Lys, S-adenosylhomocysteine, and 5'-deoxy-5'-methylthioadenosine | Arabidopsis thaliana | ? | - |
? | |
additional information | the bifunctional enzyme catalyzes both diaminopelargonic acid aminotransferase and dethiobiotin synthetase reactions in vitro. In the course of the reaction, the diaminopelargonic acid intermediate is directly transferred from the diaminopelargonic acid aminotransferase active site to the dethiobiotin synthetase active site. The overall reaction is rate limited by the diaminopelargonic acid aminotransferase activity | Arabidopsis thaliana | ? | - |
? | |
additional information | the BIO3-BIO1 fusion protein is the sole protein form produced by the BIO3-BIO1 locus in Arabidopsis. The enzyme catalyzes both diaminopelargonic acid aminotransferase and dethiobiotin synthetase reactions in vitro. In the course of the reaction, the diaminopelargonic acid intermediate is directly transferred from the both diaminopelargonic acid aminotransferase active site to the dethiobiotin synthetase active site | Arabidopsis thaliana | ? | - |
? | |
additional information | the BIO3-BIO1 fusion protein is the sole protein form produced by the BIO3-BIO1 locus in Arabidopsis. The enzyme catalyzes both diaminopelargonic acid aminotransferase and dethiobiotin synthetase reactions in vitro. In the course of the reaction, the diaminopelargonic acid intermediate is directly transferred from the both diaminopelargonic acid aminotransferase active site to the dethiobiotin synthetase active site. The enzyme exhibits a kinetic cooperativity with respect to all tested substrates and for both reactions | Arabidopsis thaliana | ? | - |
? | |
S-adenosyl-L-methionine + 8-amino-7-oxononanoate | - |
Arabidopsis thaliana | S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 90000, SDS-PAGE | Arabidopsis thaliana |
More | the BIO3-BIO1 fusion protein is the sole protein form produced by the BIO3-BIO1 locus in Arabidopsis. The enzyme catalyzes both diaminopelargonic acid aminotransferase and dethiobiotin synthetase reactions in vitro | Arabidopsis thaliana |
Synonyms | Comment | Organism |
---|---|---|
Bio3-Bio1 | - |
Arabidopsis thaliana |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.001 | - |
S-adenosyl-L-methionine | mutant F326Y, pH 8.6, 37°C | Arabidopsis thaliana | |
0.0012 | - |
S-adenosyl-L-methionine | wild-type, pH 8.6, 37°C | Arabidopsis thaliana |