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(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
-
?
2,3-butanedione + (S)-(-)-1-phenylpropylamine
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine
?
2,3-pentanedione + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2-oxo-2-phenylacetaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
benzaldehyde + (S)-(-)-1-phenylethylamine
propiophenone + ?
-
-
-
?
DL-lysine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
-
L-lysine is preferred
-
-
?
glyoxylate + (S)-(-)-1-phenylethylamine
?
-
-
-
?
hexanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
isobutyraldehyde + (S)-(-)-1-phenylethylamine
acetophenone + ?
molecular docking study
-
-
?
isobutyraldehyde + (S)-(-)-1-phenylpropylamine
acetophenone + ?
-
-
-
?
pimeloyl-[acyl-carrier protein] + L-alanine
8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
propanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
pyruvaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
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-(methylsulfanyl)-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 + sinefungin
S-adenosyl-4-methylthio-2-oxobutanoate + ?
additional information
?
-
2,3-butanedione + (S)-(-)-1-phenylpropylamine

?
-
-
-
?
2,3-butanedione + (S)-(-)-1-phenylpropylamine
?
-
-
-
?
2,3-butanedione + (S)-(-)-1-phenylpropylamine
?
-
-
-
?
2,3-butanedione + (S)-(-)-1-phenylpropylamine
?
-
-
-
?
2,3-butanedione + (S)-(-)-1-phenylpropylamine
?
-
-
-
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine

?
-
-
-
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-dihydroxypropanaldehyde + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine

?
-
-
-
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine
?
-
-
-
?
2,3-hexanedione + (S)-(-)-1-phenylethylamine
?
-
-
-
?
pimeloyl-[acyl-carrier protein] + L-alanine

8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
-
-
-
?
pimeloyl-[acyl-carrier protein] + L-alanine
8-amino-7-oxononanoate + CO2 + holo-[acyl-carrier protein]
-
-
-
?
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-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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
-
-
-
?
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-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
?
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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
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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. The enzyme exhibits a kinetic cooperativity with respect to all tested substrates and for both reactions
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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. The enzyme exhibits a kinetic cooperativity with respect to all tested substrates and for both reactions
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additional information
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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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additional information
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the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
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additional information
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the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
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additional information
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the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
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additional information
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the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
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additional information
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the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
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additional information
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the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
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additional information
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the enzyme also catalzes the reaction of EC 2.6.1.19, the 4-aminobutanoate transaminase reaction, but with much less activity compared to the adenosylmethionine-8-amino-7-oxononanoate aminotransferase activity. Substrate specificity analysis
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additional information
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7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
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additional information
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7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
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additional information
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7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
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additional information
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7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
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additional information
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7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
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additional information
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7,8-diaminopelargonic acid transaminase (synthase), previously considered to be highly specific, is able to convert (S)-(-)-1-phenylethylamine and a number of aldehydes and diketones. Only a weak activity towards pyruvate is detected. The enzyme shows (S)-amine transaminase activity. The Pcryo361 affinity towards (S)-(-)-1-phenylethylamine arises from the recognition of the hydrophobic parts of the specific substrates, S-adenosyl-L-methionine and 7-keto-8-aminopelargonic acid, and from the flexibility of the active site. Analysis of the half-transamination reaction measuring a decrease in aldimine concentration in the presence of different concentrations of S-adenosyl-L-methionine, (S)-(-)-1-phenylethylamine, L-lysine, and (S)-(-)-1,2-diaminopropane, substrate specificity of enzyme Pcryo361 in the half and the overall reactions, overview. No activity towards 2,4-pentanedione, 2-oxobutyrate, or acetone as amine acceptor substrates, poor activity with pyruvate, no activity with (R)-(-)-1-phenylethylamine as amine donor substrate
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