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Information on EC 2.6.1.62 - adenosylmethionine-8-amino-7-oxononanoate transaminase and Organism(s) Arabidopsis thaliana and UniProt Accession B0F481
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EC Tree
2.6.1.62 adenosylmethionine-8-amino-7-oxononanoate transaminaseIUBMB Comments
A pyridoxal 5'-phosphate enzyme. S-adenosylhomocysteine can also act as donor.
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Word Map
- 2.6.1.62
- biotin
- tuberculosis
-
dapas
- analysis
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quinonoid
- dethiobiotin
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antepenultimate
- pyridoxal
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auxotrophic
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transamination
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5'-phosphate-dependent
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half-reaction
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bicistronic
- s-adenosylmethionine
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plp-dependent
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biotinylated
- pimeloyl-coa
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alpha-amino
- biotechnology
- pharmacology
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
Synonyms
7,8-diaminopelargonic acid synthase, bio3-bio1, dapa aminotransferase, 7,8-diaminopelargonic acid transaminase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
7,8-diaminononanoate transaminase
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-
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7,8-diaminopelargonic acid aminotransferase
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-
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7-keto-8-aminopelargonic acid aminotransferase
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7-keto-8-aminopelargonic acid-7,8-diaminopelargonic acid aminotransferase
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DAPA aminotransferase
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DAPA synthase
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DAPA transaminase
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diaminopelargonate synthase
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synthase, diaminopelargonate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:8-amino-7-oxononanoate aminotransferase
A pyridoxal 5'-phosphate enzyme. S-adenosylhomocysteine can also act as donor.
CAS REGISTRY NUMBER
COMMENTARY
37259-71-5
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
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-
-
?
additional information
?
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no substrates: L-Asp, L-Glu, L-Met, L-Lys, S-adenosylhomocysteine, and 5'-deoxy-5'-methylthioadenosine
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-
?
additional information
?
-
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no substrates: L-Asp, L-Glu, L-Met, L-Lys, S-adenosylhomocysteine, and 5'-deoxy-5'-methylthioadenosine
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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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
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-
?
additional information
?
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-
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
-
-
?
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
-
-
?
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
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
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
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-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0046
8-Amino-7-oxononanoate
mutant F326Y, K0.5 value, Hill coefficient 1.36, pH 8.6, 37°C
0.0048
8-Amino-7-oxononanoate
wild-type, K0.5 value, Hill coefficient 1.29, pH 8.6, 37°C
0.6 - 3
S-adenosyl-L-methionine
wild-type, K0.5 value, Hill coefficient 1.34, pH 8.6, 37°C
1.65
S-adenosyl-L-methionine
mutant F326Y, K0.5 value, Hill coefficient 1.23, pH 8.6, 37°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional dethiobiotin synthetase/diaminopelargonic acid aminotransferase
UniProt
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
UniProt
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BIODA_ARATH
833
0
91935
Swiss-Prot
Mitochondrion (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F326Y
I793W
S360Y
F326Y
mutant improves the recombinant enzyme solubility and stability
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
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
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
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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli as truncated protein, with an N-terminal 22-residue deletion
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Plant Cell
24
1608-1625
2012
Arabidopsis thaliana (B0F481), Arabidopsis thaliana
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