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Information on EC 2.6.1.62 - adenosylmethionine-8-amino-7-oxononanoate transaminase
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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
- mycobacterium
-
dapas
- tuberculosis
- analysis
- dethiobiotin
-
quinonoid
-
antepenultimate
-
transamination
-
auxotrophic
- pyridoxal
-
alpha-amino
-
half-reaction
- s-adenosylmethionine
-
5'-phosphate-dependent
- pimeloyl-coa
-
bicistronic
- biotechnology
- pharmacology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
7,8-diaminopelargonic acid synthase, dapa aminotransferase, bio3-bio1, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
7,8-diaminopelargonic acid aminotransferase
7,8-diaminopelargonic acid synthase
bioA
DAPA AT
DAPA synthase
S-adenosyl-L-methionine:8-amino-7-oxononanoate aminotransferase
-
-
additional information
-
the enzyme is a member of fold type I PLP enzyme group, aminotransferase subclass II
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
ping-pong mechanism
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
reaction mechanism analysis, via a enzyme-pyridoxamine phosphate, a S-adenosyl-L-methionine quinonoid intermediate, the substrate structure is a major determinant of the thermodynamic and/or kinetic accessibility of the quinonoid and ketimine intermediates
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
structural basis for reaction mechanism
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
reaction mechanism, substrate binding structure, detailed reversible aminotransferase half-reaction, overview, residues Tyr17, Asp147, and conserved Tyr144 and Arg253 are important for catalysis
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
double displacement or ping pong reaction mechanism
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
ping pong kinetics, reaction mechanism, via a enzyme-pyridoxamine phosphate, a quinonoid intermediate
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
enzyme shows a Ping Pong Bi Bi kinetic mechanism with strong substrate inhibition
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
enzyme shows a Ping Pong Bi Bi kinetic mechanism with strong substrate inhibition
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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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.
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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,S)-S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
first half-reaction is reversible, the second one is irreversible, enzyme does not react with the (R,S)-diastereomer of S-adenosyl-L-methionine
i.e. 7,8-diaminopelargonic acid
-
?
DL-lysine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
-
L-lysine is preferred
-
-
?
S-2-aminoethyl-L-cysteine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
-
-
-
-
?
S-adenosyl-(5')-3-methylthiopropylamine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
decarboxylated S-adenosyl-L-methionine is as reactive as S-adenosyl-L-methionine
-
-
r
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoic acid
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 7,8-diketopelargonic acid
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
enzyme only uses (S)-8-amino-7-oxononanoate as substrate
-
-
?
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
enzyme only uses (S)-8-amino-7-oxononanoate as substrate
-
-
?
S-adenosyl-L-methionine + 7,8-diketopelargonic acid
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 7,8-diketopelargonic acid
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
-
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
1% of the activity of 8-amino-7-oxononanoate
-
-
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
1% of the activity of 8-amino-7-oxononanoate
-
-
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
S-adenosyl-4-methylthio-2-oxobutanoate may be decomposed nonenzymatically to form 5'-methylthioadenosine and 2-oxo-3-butenoic acid
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
S-adenosyl-4-methylthio-2-oxobutanoate may be decomposed nonenzymatically to form 5'-methylthioadenosine and 2-oxo-3-butenoic acid
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
synonym: 7,8-diaminopelargonic acid
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
1% of the activity of 8-amino-7-oxononanoate
-
-
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
1% of the activity of 8-amino-7-oxononanoate
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
enzyme is obligate catalyzing the second step in the biosynthesis of vitamin H, i.e. biotin
-
-
r
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
involved in the biosynthesis of biotin
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
second of 4 steps in the biosynthesis of vitamin H, i.e. biotin
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
second of 4 steps in the biosynthesis of vitamin H, i.e. biotin
-
-
r
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
first half-reaction is reversible, the second one is irreversible
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
stereospecific amination
-
-
r
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
the aminotransferase half-reaction is reversible, substrate binding structure
-
-
r
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
involved in the biosynthesis of biotin
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
no substrates: S-adenosyl-L-ethionine, S-adenosyl-L-homocysteine, S-adenosyl-L-(2-4-methylthio)butyric acid, S-methyl-L-methionine, adenosine, methionine
S-adenosyl-4-methylthio-2-oxobutanoate may be decomposed nonenzymatically to form 5'-methylthioadenosine and 2-oxo-3-butenoic acid, synonym: 7,8-diaminopelargonic acid
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
transfer of alpha-amino group from S-adenosyl-L-methionine to KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
S-adenosyl-4-methylthio-2-oxobutanoate may be decomposed nonenzymatically to form 5'-methylthioadenosine and 2-oxo-3-butenoic acid
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
S-adenosyl-4-methylthio-2-oxobutanoate may be decomposed nonenzymatically to form 5'-methylthioadenosine and 2-oxo-3-butenoic acid
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
synonym: 7,8-diaminopelargonic acid
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
ping pong bi bi kinetic mechanism with strong substrate inhibition
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + sinefungin
S-adenosyl-4-methylthio-2-oxobutanoate + ?
-
-
-
?
S-adenosyl-L-methionine + sinefungin
S-adenosyl-4-methylthio-2-oxobutanoate + ?
-
-
-
?
additional information
?
-
-
no substrates: L-Asp, L-Glu, L-Met, L-Lys, S-adenosylhomocysteine, and 5'-deoxy-5'-methylthioadenosine
-
-
-
additional information
?
-
no substrates: L-Asp, L-Glu, L-Met, L-Lys, S-adenosylhomocysteine, and 5'-deoxy-5'-methylthioadenosine
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
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
-
-
-
additional information
?
-
-
enzyme does not utilize S-adenosyl-L-methionine, Nalpha-acetyl-L-lysine, Nepsilon-acetyl-L-lysine, Nepsilon-methyl-L-lysine, glycine-lysine dipeptide, lysine-glycine dipeptide, and diaminopimelic acid as amino donors
-
-
-
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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
DL-lysine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
-
L-lysine is preferred
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
enzyme is obligate catalyzing the second step in the biosynthesis of vitamin H, i.e. biotin
-
-
r
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
involved in the biosynthesis of biotin
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
second of 4 steps in the biosynthesis of vitamin H, i.e. biotin
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
second of 4 steps in the biosynthesis of vitamin H, i.e. biotin
-
-
r
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
involved in the biosynthesis of biotin
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
Bacillus roseus IAM 1257
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
-
biotin synthesis
-
-
-
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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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxamine 5'-phosphate
-
active as cofactor
pyridoxamine 5'-phosphate
-
active as cofactor
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(R)-8-amino-7-oxononanoate
binds both to the pyridoxal 5'-phosphate form and to the pyridoxamine 5'-phosphate form by forming specific hydrogen bonds with residue T309 and the phosphate group of the cofactor
2-hydrazinyl-1,3-benzothiazole
reversible covalent inhibitor
3-(cis-4-aminocyclohexa-2,5-dien-1-yl)propan-1-ol
suicide substrate, compound at 0.1 mg/l completely inhibits the growth of an Escherichia coli C268bioA mutant strain transformed with a plasmid expressing the Myobaterium tuberculosis bioA gene, coding for diaminopelargonic acid aminotransferase; suicide substrate, irreversible inhibition
4-(1H-imidazol-1-yl)benzamide
inhibitor identified by fragment library biophysical screening, induces Trp64 and Trp65 changes to widen the binding site, but also perturbs Tyr25. Binding induces a shift in melting temperature of +4.1 degrees
5-(pyridin-2-yl)thiophene-2-carboxamide
inhibitor identified by fragment library biophysical screening, induces a strong remodeling of the active site. Compound can inhibit the growth of virulent strains in biotin-deprived media. Binding induces a shift in melting temperature of +6.3 degrees
cis-amiclenomycin
-
and analogues, overview, irreversible inactivation, kinact. 0.4 min-1, little or no inhibition by the trans-compound, overview
N-methyl-1-[4-(1H-pyrazol-1-ylmethyl)phenyl]methanamine
inhibitor identified by fragment library biophysical screening, binding is purely enthalpie-driven. Binding induces a shift in melting temperature of +5.3 degrees
additional information
-
no inhibition by the (R,S)-diastereomer of S-adenosyl-L-methionine
-
7-Keto-8-aminopelargonic acid
-
competitive with adenosyl-L-methionine
8-amino-7-oxooctanoic acid
achiral analog of 8-amino-7-oxononanoate
amiclenomycin
suicide substrate; suicide substrate, irreversible inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.7
sinefungin
pH 7.5, temperature not specified in the publication
0.0046
8-Amino-7-oxononanoate
mutant F326Y, K0.5 value, Hill coefficient 1.36, pH 8.6, 37°C; mutant F326Y, 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; wild-type, pH 8.6, 37°C
0.1
S-adenosyl-(5')-3-methylthiopropylamine
pH 9.0, recombinant mutant R253K
0.75
S-adenosyl-(5')-3-methylthiopropylamine
pH 9.0, recombinant wild-type enzyme
0.45
S-adenosyl-L-methionine
pH 7.5, temperature not specified in the publication
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
additional information
additional information
-
kinetics, first-order rate constant for the first half-reaction at saturation, the transamination reaction passes slowly due to either ketimine formation or its hydrolysis being hindered
-
additional information
additional information
-
single turnover reactions, stopped-flow, wild-type and mutant enzymes
-
additional information
additional information
single turnover reactions, stopped-flow, wild-type and mutant enzymes
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.016
S-adenosyl-(5')-3-methylthiopropylamine
pH 9.0, recombinant wild-type enzyme and mutant R253K
0.009
sinefungin
pH 7.5, temperature not specified in the publication
1.3
8-Amino-7-oxononanoate
pH 9.0, recombinant mutant R253A; pH 9.0, recombinant mutant R253K
0.012
S-adenosyl-L-methionine
pH 7.5, temperature not specified in the publication
additional information
additional information
single turnover reactions
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.03
S-adenosyl-L-methionine
pH 7.5, temperature not specified in the publication
0.013
sinefungin
pH 7.5, temperature not specified in the publication
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0017
(R)-8-amino-7-oxononanoate
binding to the the pyridoxamine 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
0.0059
(R)-8-amino-7-oxononanoate
binding to the the pyridoxal 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
0.0017
(R)-8-amino-7-oxononanoic acid
bound to the pyridoxamine 5'-phosphate form, 100 mM EPPS buffer, pH 8.6
0.0059
(R)-8-amino-7-oxononanoic acid
bound to the pyridoxal 5'-phosphate enzyme form, 100 mM EPPS buffer, pH 8.6
0.014
3-(cis-4-aminocyclohexa-2,5-dien-1-yl)propan-1-ol
pH 8.6, 37°C
0.02
3-(cis-4-aminocyclohexa-2,5-dien-1-yl)propan-1-ol
; pH 8.6, 37°C
0.0009
8-amino-7-oxooctanoate
bound to the pyridoxamine 5'-phosphate form, 100 mM EPPS buffer, pH 8.6
0.0042
8-amino-7-oxooctanoate
bound to the pyridoxal 5'-phosphate form, 100 mM EPPS buffer, pH 8.6
0.0009
8-amino-7-oxooctanoic acid
binding to the the pyridoxamine 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
0.0042
8-amino-7-oxooctanoic acid
binding to the the pyridoxal 5'-phosphate form of enzyme, pH not specified in the publication, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 50
-
25°C: about 65% of activity maximum, 50°C: about 60% of activity maximum
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional dethiobiotin synthetase/diaminopelargonic acid aminotransferase; 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
brenda
AJ 2635, AJ 2636
-
-
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (14595 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Escherichia coli (strain K12)
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Chromobacterium violaceum (strain ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757)
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
purified recombinant mutant enzymes Y17F, Y144F, D147N, R253A, and R253K, hanging drop method, 20°C, 10 mg/ml protein in solution mixed with equal volume of well solution containing 26-28% PEG 4000, 9-12% methylpentanediol, 100 mM HEPES, pH 7.5, microseeding, 2 days, X-ray diffraction structure determination and analysis at 1.7-2.4 A resolution, modeling
in complex with inhibitors 5-(pyridin-2-yl)thiophene-2-carboxamide, 4-(1H-imidazol-1-yl)benzamide, and N-methyl-1-[4-(1H-pyrazol-1-ylmethyl)phenyl]methanamine
in complex with substrate 7-oxo-8-aminopelargonic acid and in complex with inhibitors 1-(1,3-benzothiazol-2-yl)methanamine and 2-hydrazinyl-1,3-benzothiazole. The side chains of Tyr25, Trp65, Arg400, and Tyr407 are shown to be quite flexible. Small molecule binding induces unexpected conformational remodeling in the substrate binding site
to 2.2 A resolution, by molecular replacement, and superimposition of the structures bound either to the S-adenosyl-L-methionine analog sinefungin or to 7-oxo-8-aminopelargonic acid. Comparison to structure of the Bacillus subtilis enzyme, EC 2.5.1.105
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F326Y
mutant improves the recombinant enzyme solubility and stability; no major impact on kinetic parameters
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; 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
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; 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
D147N
site-directed mutagenesis, mutation of an active site residue, inactive mutant
R253A
site-directed mutagenesis, altered kinetics, highly increased Km for S-adenosyl-L-methionine compared to the wild-type enzyme
R253K
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
R253M
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
R253Q
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
R391A
-
increased Km for 7,8-diaminopelargonic acid, no significantly altered crystal structure
Y144F
site-directed mutagenesis, mutation of an active site residue, highly increased Km for S-adenosyl-L-methionine, highly reduced activity compared to the wild-type enzyme
Y17F
site-directed mutagenesis, mutation of an active site residue, highly reduced activity compared to the wild-type enzyme
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
67
melting temperature, in complex with inhibitor 2-hydrazinyl-1,3-benzothiazole
78
melting temperature, in complex with inhibitor 1-(1,3-benzothiazol-2-yl)methanamine
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant soluble N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
; expression in Escherichia coli as truncated protein, with an N-terminal 22-residue deletion
overexpression as mostly insoluble, N-terminally His6-tagged enzyme in Escherichia coli
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
-
evaluation of biotin overproduction, biotin production by Bacillus subtilis fermentation can be optimized by addition of exogenous lysine or mutational deregulation of lysine in the producing strain
pharmacology
-
enzyme is a potential drug target in tuberculosis treatment
analysis
analytical method to measure the enantiomeric excess of substrate 8-amino-7-oxononanoic acid, based on the derivatization of its amine function, by orthophtalaldehyde and N-acetyl-L-cysteine, followed by high pressure liquid chromatography separation. Using this methodology and enantiopure samples of 8-amino-7-oxononanoic acid, it appears that racemization of 8-amino-7-oxononanoic acid occurs rapidly with half-lives from 1 to 8 h, not only in 4 M HCl but also in the usual pH range, from 7 to 9
analysis
microplate fluorescence assay for 7,8-diaminopelargonic acid aminotransferase that is simple, cheap, and sensitive, allowing linear detection of 7,8-diaminopelargonic acid in the range of 20 nM to 50 microM. The principle of the method is the direct detection in the enzymatic reaction mixture of the vicinal diamine 7,8-diaminopelargonic acid derivatized with ortho-phthalaldehyde and 2-mercaptoethanol; simple, cheap, and sensitive microplate fluorescence assay, allowing linear detection of 7,8-diaminopelargonic acid in the range of 20 nM to 50 microM. The principle of the method is the direct detection in the enzymatic reaction mixture of the vicinal diamine 7,8-diaminopelargonic acid derivatized with ortho-phthalaldehyde and 2-mercaptoethanol. The assay is validated with inhibitor 8-amino-7-oxopelargonic acid and adapted to microplate; simple, cheap, and sensitive microplate fluorescence assay for 7,8-diaminopelargonic acid aminotransferase activity, allowing linear detection of 7,8-diaminopelargonic acid in the range of 20 nM to 50 microM. The method relies on the direct detection in the enzymatic reaction mixture of the vicinal diamine 7,8-diaminopelargonic acid derivatized with ortho-phthalaldehyde and 2-mercaptoethanol. The assay was validated with the known inhibitor desmethyl-KAPA, i.e. 8-amino-7-oxopelargonic acid, and adapted to microplate for high-throughput screening
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
analysis
-
analytical method to measure the enantiomeric excess of substrate 8-amino-7-oxononanoic acid, based on the derivatization of its amine function, by orthophtalaldehyde and N-acetyl-L-cysteine, followed by high pressure liquid chromatography separation. Using this methodology and enantiopure samples of 8-amino-7-oxononanoic acid, it appears that racemization of 8-amino-7-oxononanoic acid occurs rapidly with half-lives from 1 to 8 h, not only in 4 M HCl but also in the usual pH range, from 7 to 9; microplate fluorescence assay for 7,8-diaminopelargonic acid aminotransferase that is simple, cheap, and sensitive, allowing linear detection of 7,8-diaminopelargonic acid in the range of 20 nM to 50 microM. The principle of the method is the direct detection in the enzymatic reaction mixture of the vicinal diamine 7,8-diaminopelargonic acid derivatized with ortho-phthalaldehyde and 2-mercaptoethanol; simple, cheap, and sensitive microplate fluorescence assay, allowing linear detection of 7,8-diaminopelargonic acid in the range of 20 nM to 50 microM. The principle of the method is the direct detection in the enzymatic reaction mixture of the vicinal diamine 7,8-diaminopelargonic acid derivatized with ortho-phthalaldehyde and 2-mercaptoethanol. The assay is validated with inhibitor 8-amino-7-oxopelargonic acid and adapted to microplate
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Izumi, Y.; Tani, Y.; Ogata, K.
Microbiological biosynthesis of biotin
Methods Enzymol.
62
326-338
1979
Bacillus roseus, Bacillus roseus IAM 1257, Corynebacterium glutamicum, Kocuria rosea, Salmonella enterica subsp. enterica serovar Typhimurium
brenda
Stoner, G.L.; Eisenberg, M.A.
Purification and properties of 7,8-diaminopelargonic acid aminotransferase
J. Biol. Chem.
250
4029-4036
1975
Escherichia coli
brenda
Izumi, Y.; Sato, K.; Tani, Y.; Ogata, K.
Biosynthesis of biotin by microorganisms. XV. 7,8-Diaminopelargonic acid aminotransferase, an enzyme involved in biotin biosynthesis by microorganisms
Agric. Biol. Chem.
39
175-181
1975
Bacillus roseus, Bacillus roseus IAM 1257, Corynebacterium glutamicum, Corynebacterium glutamicum NRRL 2311, Escherichia coli, Escherichia coli AKV 0015, Kocuria rosea, Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Izumi, Y.; Sato, K.; Tani, Y.; Ogata, K.
7,8-Diaminopelargonic acid aminotransferase, an enzyme involved in biotin biosynthesis by microorganisms
Agric. Biol. Chem.
37
2683-2684
1973
Bacillus roseus, Bacillus roseus IAM 1257, Corynebacterium glutamicum, Escherichia coli, Kocuria rosea, Salmonella enterica subsp. enterica serovar Typhimurium
-
brenda
Stoner, G.L.; Eisenberg, M.A.
Biosynthesis of 7,8-diaminopelargonic acid from 7-keto-8-aminopelargonic acid and S-adenosyl-L-methionine. The kinetics of the reaction
J. Biol. Chem.
250
4037-4043
1975
Corynebacterium glutamicum, Corynebacterium glutamicum NRRL 2311, Escherichia coli
brenda
Eisenberg, M.A.; Stoner, G.L.
7,8-Diaminopelargonic acid aminotransferase
Methods Enzymol.
62
342-347
1979
Escherichia coli
brenda
Eliot, A.C.; Sandmark, J.; Schneider, G.; Kirsch, J.F.
The dual-specific active site of 7,8-diaminopelargonic acid synthase and the effect of the R391A mutation
Biochemistry
41
12582-12589
2002
Escherichia coli
brenda
Käck, H.; Gibson, K.J.; Gatenby, A.A.; Schneider, G.; Lindqvist, Y.
Purification and preliminary x-ray crystallographic studies of recombinant 7,8-diaminopelargonic acid synthase from Escherichia coli
Acta Crystallogr. Sect. D
54
1397-1398
1998
Escherichia coli
brenda
Käck, H.; Sandmark, J.; Gibson, K.; Schneider, G.; Lindqvist, Y.
Crystal structure of diaminopelargonic acid synthase: evolutionary relationships between pyridoxal-5'-phosphate-dependent enzymes
J. Mol. Biol.
291
857-876
1999
Escherichia coli
brenda
Eliot, A.C.; Kirsch, J.F.
Avoiding the road less traveled: how the topology of enzyme-substrate complexes can dictate product selection
Acc. Chem. Res.
36
757-765
2003
Escherichia coli
brenda
Mann, S.; Marquet, A.; Ploux, O.
Inhibition of 7,8-diaminopelargonic acid aminotransferase by amiclenomycin and analogues
Biochem. Soc. Trans.
33
802-805
2005
Escherichia coli, Mycobacterium tuberculosis
brenda
Sandmark, J.; Eliot, A.C.; Famm, K.; Schneider, G.; Kirsch, J.F.
Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis
Biochemistry
43
1213-1222
2004
Escherichia coli, Escherichia coli (P12995)
brenda
Van Arsdell, S.W.; Perkins, J.B.; Yocum, R.R.; Luan, L.; Howitt, C.L.; Chatterjee, N.P.; Pero, J.G.
Removing a bottleneck in the Bacillus subtilis biotin pathway: bioA utilizes lysine rather than S-adenosylmethionine as the amino donor in the KAPA-to-DAPA reaction
Biotechnol. Bioeng.
91
75-83
2005
Bacillus subtilis
brenda
Breen, R.S.; Campopiano, D.J.; Webster, S.; Brunton, M.; Watt, R.; Baxter, R.L.
The mechanism of 7,8-diaminopelargonate synthase; the role of S-adenosylmethionine as the amino donor
Org. Biomol. Chem.
1
3498-3499
2003
Escherichia coli
brenda
Mann, S.; Ploux, O.
7,8-Diaminoperlargonic acid aminotransferase from Mycobacterium tuberculosis, a potential therapeutic target. Characterization and inhibition studies
FEBS J.
273
4778-4789
2006
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis ATCC 25618 (P9WQ81)
brenda
Mann, S.; Colliandre, L.; Labesse, G.; Ploux, O.
Inhibition of 7,8-diaminopelargonic acid aminotransferase from Mycobacterium tuberculosis by chiral and achiral anologs of its substrate: biological implications
Biochimie
91
826-834
2009
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis ATCC 25618 (P9WQ81)
brenda
Dey, S.; Lane, J.M.; Lee, R.E.; Rubin, E.J.; Sacchettini, J.C.
Structural characterization of the Mycobacterium tuberculosis biotin biosynthesis enzymes 7,8-diaminopelargonic acid synthase and dethiobiotin synthetase
Biochemistry
49
6746-6760
2010
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WQ80), Mycobacterium tuberculosis CDC 1551 (P9WQ80)
brenda
Mann, S.; Eveleigh, L.; Lequin, O.; Ploux, O.
A microplate fluorescence assay for DAPA aminotransferase by detection of the vicinal diamine 7,8-diaminopelargonic acid
Anal. Biochem.
432
90-96
2013
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis ATCC 25618 (P9WQ81)
brenda
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, Arabidopsis thaliana (B0F481)
brenda
Shi, C.; Aldrich, C.C.
Design and synthesis of potential mechanism-based inhibitors of the aminotransferase BioA involved in biotin biosynthesis
J. Org. Chem.
77
6051-6058
2012
Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis ATCC 25618 (P9WQ81)
brenda
Dai, R.; Wilson, D.J.; Geders, T.W.; Aldrich, C.C.; Finzel, B.C.
Inhibition of Mycobacterium tuberculosis transaminase BioA by aryl hydrazines and hydrazides
ChemBioChem
15
575-586
2014
Mycobacterium tuberculosis, Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis H37Rv (P9WQ81)
brenda
Dai, R.; Geders, T.W.; Liu, F.; Park, S.W.; Schnappinger, D.; Aldrich, C.C.; Finzel, B.C.
Fragment-based exploration of binding site flexibility in Mycobacterium tuberculosis BioA
J. Med. Chem.
58
5208-5217
2015
Mycobacterium tuberculosis (P9WQ81), Mycobacterium tuberculosis H37Rv (P9WQ81)
brenda
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