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Literature summary extracted from

  • Cobessi, D.; Dumas, R.; Pautre, V.; Meinguet, C.; Ferrer, J.L.; Alban, C.
    Biochemical and structural characterization of the Arabidopsis bifunctional enzyme dethiobiotin synthetase-diaminopelargonic acid aminotransferase: evidence for substrate channeling in biotin synthesis (2012), Plant Cell, 24, 1608-1625.
    View publication on PubMedView publication on EuropePMC

Application

EC Number Application Comment Organism
2.6.1.62 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(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.62
-
 Arabidopsis thaliana
2.6.1.62 expression in Escherichia coli as truncated protein, with an N-terminal 22-residue deletion Arabidopsis thaliana

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.62 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
2.6.1.62 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

EC Number Protein Variants Comment Organism
2.6.1.62 F326Y no major impact on kinetic parameters Arabidopsis thaliana
2.6.1.62 F326Y mutant improves the recombinant enzyme solubility and stability Arabidopsis thaliana
2.6.1.62 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
2.6.1.62 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
2.6.1.62 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
2.6.1.62 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.62 0.0046
-
 8-Amino-7-oxononanoate mutant F326Y, pH 8.6, 37°C Arabidopsis thaliana
2.6.1.62 0.0046
-
 8-Amino-7-oxononanoate mutant F326Y, K0.5 value, Hill coefficient 1.36, pH 8.6, 37°C Arabidopsis thaliana
2.6.1.62 0.0048
-
 8-Amino-7-oxononanoate wild-type, pH 8.6, 37°C Arabidopsis thaliana
2.6.1.62 0.0048
-
 8-Amino-7-oxononanoate wild-type, K0.5 value, Hill coefficient 1.29, pH 8.6, 37°C Arabidopsis thaliana
2.6.1.62 0.6 3 S-adenosyl-L-methionine wild-type, K0.5 value, Hill coefficient 1.34, pH 8.6, 37°C Arabidopsis thaliana
2.6.1.62 0.63
-
 S-adenosyl-L-methionine wild-type, pH 8.6, 37°C Arabidopsis thaliana
2.6.1.62 1.63
-
 S-adenosyl-L-methionine mutant F326Y, pH 8.6, 37°C Arabidopsis thaliana
2.6.1.62 1.65
-
 S-adenosyl-L-methionine mutant F326Y, K0.5 value, Hill coefficient 1.23, pH 8.6, 37°C Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.6.1.62 mitochondrion
-
 Arabidopsis thaliana 5739
-
2.6.1.62 mitochondrion mitochondrial matrix Arabidopsis thaliana 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.6.1.62 90000
-
 x * 90000, SDS-PAGE Arabidopsis thaliana

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.62 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

EC Number Organism UniProt Comment Textmining
2.6.1.62 Arabidopsis thaliana B0F481 bifunctional dethiobiotin synthetase/diaminopelargonic acid aminotransferase
-
2.6.1.62 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 and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.62 additional information no substrates: L-Asp, L-Glu, L-Met, L-Lys, S-adenosylhomocysteine, and 5'-deoxy-5'-methylthioadenosine Arabidopsis thaliana ?
-
 ?
2.6.1.62 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 ?
-
 ?
2.6.1.62 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 ?
-
 ?
2.6.1.62 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 ?
-
 ?
2.6.1.62 S-adenosyl-L-methionine + 8-amino-7-oxononanoate
-
 Arabidopsis thaliana S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
 ?

Subunits

EC Number Subunits Comment Organism
2.6.1.62 ? x * 90000, SDS-PAGE Arabidopsis thaliana
2.6.1.62 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

EC Number Synonyms Comment Organism
2.6.1.62 Bio3-Bio1
-
 Arabidopsis thaliana

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.62 0.001
-
 S-adenosyl-L-methionine mutant F326Y, pH 8.6, 37°C Arabidopsis thaliana
2.6.1.62 0.0012
-
 S-adenosyl-L-methionine wild-type, pH 8.6, 37°C Arabidopsis thaliana