Information on EC 2.6.1.62 - adenosylmethionine-8-amino-7-oxononanoate transaminase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
2.6.1.62
-
RECOMMENDED NAME
GeneOntology No.
adenosylmethionine-8-amino-7-oxononanoate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
ping-pong mechanism
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
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-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
structural basis for reaction mechanism
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
reaction mechanism, substrate binding structure, detailed reversible aminotransferase half-reaction, overview, residues Tyr17, Asp147, and conserved Tyr144 and Arg253 are important for catalysis
-, P12995
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
double displacement or ping pong reaction mechanism
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
ping pong kinetics, reaction mechanism, via a enzyme-pyridoxamine phosphate, a quinonoid intermediate
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
enzyme shows a 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
show the reaction diagram
enzyme shows a Ping Pong Bi Bi kinetic mechanism with strong substrate inhibition
Mycobacterium tuberculosis ATCC 25618
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
biotin biosynthesis from 8-amino-7-oxononanoate I
-
Biotin metabolism
-
Metabolic pathways
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7,8-diaminononanoate transaminase
-
-
-
-
7,8-diaminopelargonate synthase
-
-
7,8-diaminopelargonic acid aminotransferase
-
-
-
-
7,8-diaminopelargonic acid aminotransferase
-
-
7,8-diaminopelargonic acid aminotransferase
-
-
7,8-diaminopelargonic acid aminotransferase
P9WQ81
-
7,8-diaminopelargonic acid aminotransferase
Mycobacterium tuberculosis ATCC 25618
P9WQ81
-
-
7,8-diaminopelargonic acid synthase
-
-
7,8-diaminopelargonic acid synthase
P12995
-
7,8-diaminoperlargonic acid aminotransferase
-
-
7-keto-8-aminopelargonic acid aminotransferase
-
-
-
-
7-keto-8-aminopelargonic acid-7,8-diaminopelargonic acid aminotransferase
-
-
-
-
Bio3-Bio1
B0F481
-
DAPA amino transferase
-
-
DAPA aminotransferase
-
-
-
-
DAPA AT
-
-
DAPA AT
Mycobacterium tuberculosis ATCC 25618
P9WQ81
-
-
DAPA synthase
-
-
-
-
DAPA synthase
-
-
DAPA synthase
P12995
-
DAPA transaminase
-
-
-
-
diaminopelargonate synthase
-
-
-
-
S-adenosyl-L-methionine:8-amino-7-oxononanoate aminotransferase
-
-
synthase, diaminopelargonate
-
-
-
-
diaminoperlargonic acid aminotransferase
-
-
additional information
-
the enzyme is a member of fold type I PLP enzyme group, aminotransferase subclass II
CAS REGISTRY NUMBER
COMMENTARY
37259-71-5
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
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
Manually annotated by BRENDA team
Bacillus roseus
IAM 1257
-
-
Manually annotated by BRENDA team
Bacillus roseus IAM 1257
IAM 1257
-
-
Manually annotated by BRENDA team
gene bioA, strains BI282 and BI603, no activity in strain BI9
-
-
Manually annotated by BRENDA team
Corynebacterium glutamicum NRRL 2311
NRRL 2311
-
-
Manually annotated by BRENDA team
AKV 0015
-
-
Manually annotated by BRENDA team
derepressed for the enzymes of biotin operon; regulatory mutant
-
-
Manually annotated by BRENDA team
regulatory mutant
-
-
Manually annotated by BRENDA team
Escherichia coli AKV 0015
AKV 0015
-
-
Manually annotated by BRENDA team
Mycobacterium tuberculosis ATCC 25618
-
UniProt
Manually annotated by BRENDA team
Mycobacterium tuberculosis CDC 1551
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
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
show the reaction diagram
-
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
-
?
S-2-aminoethyl-L-cysteine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
show the reaction diagram
-
-
-
-
?
S-adenosyl-(5')-3-methylthiopropylamine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
show the reaction diagram
-, P12995
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
show the reaction diagram
Mycobacterium tuberculosis, Mycobacterium tuberculosis ATCC 25618
-
enzyme only uses (S)-8-amino-7-oxononanoate as substrate
-
-
?
S-adenosyl-L-methionine + (S)-8-amino-7-oxononanoic acid
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 7,8-diketopelargonic acid
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + 7,8-diketopelargonic acid
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
-
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
show the reaction diagram
-
-
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
show the reaction diagram
-
-
synonym: 7,8-diaminopelargonic acid
?
S-adenosyl-L-methionine + 7-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
Escherichia coli AKV 0015, Corynebacterium glutamicum NRRL 2311
-
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
show the reaction diagram
Corynebacterium glutamicum NRRL 2311
-
1% of the activity of 8-amino-7-oxononanoate
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-, B0F481
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
P9WQ81
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
P9WQ80
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
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
show the reaction diagram
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
Bacillus roseus
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
P9WQ81
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
show the reaction diagram
Escherichia coli AKV 0015
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
Escherichia coli AKV 0015
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
Corynebacterium glutamicum NRRL 2311
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
Corynebacterium glutamicum NRRL 2311
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
Corynebacterium glutamicum NRRL 2311
-
synonym: 7-keto-8-aminopelargonic acid, KAPA
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
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
show the reaction diagram
Bacillus roseus IAM 1257
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
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
show the reaction diagram
Bacillus roseus IAM 1257
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
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
show the reaction diagram
Bacillus roseus IAM 1257
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
Mycobacterium tuberculosis CDC 1551
P9WQ80
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
Mycobacterium tuberculosis ATCC 25618
P9WQ81
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
show the reaction diagram
-
-
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
show the reaction diagram
-
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
show the reaction diagram
-
involved in the biosynthesis of biotin
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
show the reaction diagram
-
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
show the reaction diagram
-, P12995
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
show the reaction diagram
-
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
show the reaction diagram
-
stereospecific amination
-
-
r
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
show the reaction diagram
-, P12995
the aminotransferase half-reaction is reversible, substrate binding structure
-
-
r
S-adenosyl-L-methionine + sinefungin
S-adenosyl-4-methylthio-2-oxobutanoate + ?
show the reaction diagram
Mycobacterium tuberculosis, Mycobacterium tuberculosis CDC 1551
P9WQ80
-
-
-
?
DL-lysine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
show the reaction diagram
-
L-lysine is preferred
-
-
?
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
-
-
-
additional information
?
-
-, B0F481
no substrates: L-Asp, L-Glu, L-Met, L-Lys, S-adenosylhomocysteine, and 5'-deoxy-5'-methylthioadenosine
-
-
-
additional information
?
-
-, B0F481
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
?
-
-, B0F481
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
?
-
-, B0F481
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
Bacillus roseus
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
show the reaction diagram
-
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
show the reaction diagram
-
involved in the biosynthesis of biotin
-
-
?
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
show the reaction diagram
-
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
show the reaction diagram
-, P12995
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 + 7,8-diaminononanoate
show the reaction diagram
Escherichia coli AKV 0015, Corynebacterium glutamicum NRRL 2311
-
biotin synthesis
-
-
-
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
Bacillus roseus IAM 1257
-
biotin synthesis
-
-
-
DL-lysine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
show the reaction diagram
-
L-lysine is preferred
-
-
?
additional information
?
-
-, B0F481
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
-
-
-
COFACTOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
Bacillus roseus
-
cofactor
pyridoxal 5'-phosphate
-
cofactor; Km: 0.00083 mM
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
cofactor
pyridoxal 5'-phosphate
-
cofactor; Km: 0.032 mM
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-, P12995
i.e. vitamin B6, dependent on
pyridoxal 5'-phosphate
-
-
pyridoxal 5'-phosphate
-
dependent on
pyridoxal 5'-phosphate
-
-
pyridoxamine 5'-phosphate
Bacillus roseus
-
active as cofactor
pyridoxamine 5'-phosphate
-
active as cofactor; Km: 0.0012 mM
pyridoxamine 5'-phosphate
-
active as cofactor
pyridoxamine 5'-phosphate
-
active as cofactor
pyridoxamine 5'-phosphate
-
active as cofactor; Km: 0.021 mM
pyridoxamine 5'-phosphate
-
-
S-adenosyl-L-methionine
P9WQ80
-
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
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
-
(R)-8-amino-7-oxononanoic acid
-
potent inhibitor
3-(4-aminocyclopent-2-en-1-yl)propan-1-ol
-
-
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
7-amino-8-oxononanoate
-
2 mM
7-amino-8-oxononanoate
-
-
7-Keto-8-aminopelargonic acid
-
substrate inhibition above 0.1 mM
7-Keto-8-aminopelargonic acid
-
-
7-Keto-8-aminopelargonic acid
-
competitive with adenosyl-L-methionine
7-Keto-8-aminopelargonic acid
-
-
8-Amino-7-oxononanoate
-
-
8-Amino-7-oxononanoate
-
substrate inhibition above 0.08 mM
8-Amino-7-oxononanoate
-
; substrate inhibition
8-amino-7-oxooctanoate
-
potent inhibitor
8-amino-7-oxooctanoic acid
-
achiral analog of 8-amino-7-oxononanoate
8-amino-7-oxopelargonic acid
-
;
-
adenosine
-
5 mM
amiclenomycin
-
and analogues
amiclenomycin
-
-
amiclenomycin
-
suicide substrate; suicide substrate, irreversible inhibition
cis-amiclenomycin
-
and analogues, overview, irreversible inactivation, kinact. 0.4 min-1, little or no inhibition by the trans-compound, overview
Co2+
-
94% inhibition at 1 mM
HgCl2
-
100% inhibition at 1 mM
hydroxylamine
-
100% inhibition at 1 mM
Isoniazid
-
94% inhibition at 1 mM
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
100% inhibition at 1 mM
phenylhydrazine
-
100% inhibition at 1 mM
S-Adenosyl-L-(2-hydroxy-4-methylthio)butyric acid
-
2.5 mM
S-Adenosyl-L-(2-hydroxy-4-methylthio)butyric acid
-
-
S-adenosyl-L-ethionine
-
2 mM
S-adenosyl-L-ethionine
-
-
S-adenosyl-L-homocysteine
-
5 mM
S-Inosyl-L-(2-hydroxy-4-methylthio)butyric acid
-
2 mM
Semicarbazide
-
100% inhibition at 1 mM
additional information
-
no inhibition by the (R,S)-diastereomer of S-adenosyl-L-methionine
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.001
-
7-amino-8-oxononanoate
-
pH 8.5, 37C
1.1
-
7-amino-8-oxononanoate
-
pH 8, 37C
0.0006
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant mutant R253M
0.0008
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant mutant R253K
0.001
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant wild-type enzyme
0.0012
-
8-Amino-7-oxononanoate
-
pH 8.5, 37C
0.0012
-
8-Amino-7-oxononanoate
-
native enzyme
0.0014
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant mutant R253Q
0.002
-
8-Amino-7-oxononanoate
-
pH 9, 25C, wild-type enzyme
0.0022
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant mutant R253A
0.0038
-
8-Amino-7-oxononanoate
-
; pH 8.6, 37C
0.0046
-
8-Amino-7-oxononanoate
-, B0F481
mutant F326Y, K0.5 value, Hill coefficient 1.36, pH 8.6, 37C; mutant F326Y, pH 8.6, 37C
0.0048
-
8-Amino-7-oxononanoate
-, B0F481
wild-type, K0.5 value, Hill coefficient 1.29, pH 8.6, 37C; wild-type, pH 8.6, 37C
0.02
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant mutant Y17F
0.069
-
8-Amino-7-oxononanoate
-
pH 8, 37C
0.15
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant mutant Y144F
0.00083
-
pyridoxal 5'-phosphate
-
pH 8, 37C
0.032
-
pyridoxal 5'-phosphate
-
pH 8.5, 37C
0.0012
-
pyridoxamine 5'-phosphate
-
pH 8, 37C
0.021
-
pyridoxamine 5'-phosphate
-
pH 8.5, 37C
0.1
-
S-adenosyl-(5')-3-methylthiopropylamine
-, P12995
pH 9.0, recombinant mutant R253K
0.75
-
S-adenosyl-(5')-3-methylthiopropylamine
-, P12995
pH 9.0, recombinant wild-type enzyme
0.0002
-
S-adenosyl-L-methionine
-
pH 8.5, 37C
0.01
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant mutant R253K
0.011
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant mutant R253Q
0.063
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant mutant Y17F
0.15
-
S-adenosyl-L-methionine
-
pH 9, 25C
0.2
-
S-adenosyl-L-methionine
-
pH 8.5, 37C
0.2
-
S-adenosyl-L-methionine
-
native enzyme
0.3
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant wild-type enzyme
0.45
-
S-adenosyl-L-methionine
P9WQ80
pH 7.5, temperature not specified in the publication
0.55
-
S-adenosyl-L-methionine
-
pH 8, 37C
0.6
3
S-adenosyl-L-methionine
-, B0F481
wild-type, K0.5 value, Hill coefficient 1.34, pH 8.6, 37C
0.63
-
S-adenosyl-L-methionine
-, B0F481
wild-type, pH 8.6, 37C
0.78
-
S-adenosyl-L-methionine
-
; pH 8.6, 37C
1
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant mutant R253A
1.63
-
S-adenosyl-L-methionine
-, B0F481
mutant F326Y, pH 8.6, 37C
1.65
-
S-adenosyl-L-methionine
-, B0F481
mutant F326Y, K0.5 value, Hill coefficient 1.23, pH 8.6, 37C
3
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant mutant Y144F
0.7
-
Sinefungin
P9WQ80
pH 7.5, temperature not specified in the publication
0.23
-
8-Amino-7-oxononanoate
-
pH 9, 25C, R391A murant
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
-
kinetics
-
additional information
-
additional information
-, P12995
single turnover reactions, stopped-flow, wild-type and mutant enzymes
-
additional information
-
additional information
-
kinetics
-
additional information
-
additional information
-
kinetic analysis
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.0021
-
8-Amino-7-oxononanoate
-
pH 9, 25C, R391A mutant
0.012
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant mutant Y17F
0.013
-
8-Amino-7-oxononanoate
-
pH 9, 25C, wild-type enzyme
0.04
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant mutant Y144F
0.283
-
8-Amino-7-oxononanoate
-
pH 8.5, 37C
0.67
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant mutant R253M
0.79
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant wild-type enzyme
0.8
-
8-Amino-7-oxononanoate
-
-
1
-
8-Amino-7-oxononanoate
-
-
1.3
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant mutant R253A; pH 9.0, recombinant mutant R253K
0.016
-
S-adenosyl-(5')-3-methylthiopropylamine
-, P12995
pH 9.0, recombinant wild-type enzyme and mutant R253K
0.001
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant mutant R253A
0.001
-
S-adenosyl-L-methionine
-, B0F481
mutant F326Y, pH 8.6, 37C
0.0012
-
S-adenosyl-L-methionine
-, B0F481
wild-type, pH 8.6, 37C
0.0035
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant mutant Y17F
0.009
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant mutant R253K
0.01
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant mutant R253M
0.012
-
S-adenosyl-L-methionine
P9WQ80
pH 7.5, temperature not specified in the publication
0.016
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant wild-type enzyme
0.017
-
S-adenosyl-L-methionine
-
pH 8.6, 37C
0.02
-
S-adenosyl-L-methionine
-
-
0.06
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant mutant Y144F
0.074
-
S-adenosyl-L-methionine
-, P12995
pH 9.0, recombinant mutant R253Q
0.08
-
S-adenosyl-L-methionine
-
recombinant enzyme
0.13
-
S-adenosyl-L-methionine
-
native enzyme
0.009
-
Sinefungin
P9WQ80
pH 7.5, temperature not specified in the publication
1.7
-
8-Amino-7-oxononanoate
-, P12995
pH 9.0, recombinant mutant R253Q
additional information
-
additional information
-, P12995
single turnover reactions
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.03
-
S-adenosyl-L-methionine
P9WQ80
pH 7.5, temperature not specified in the publication
24
0.013
-
Sinefungin
P9WQ80
pH 7.5, temperature not specified in the publication
659
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
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, 37C
0.02
-
3-(cis-4-aminocyclohexa-2,5-dien-1-yl)propan-1-ol
-
; pH 8.6, 37C
0.025
-
7-Keto-8-aminopelargonic acid
-
pH 8.5, 37C
2
-
7-Keto-8-aminopelargonic acid
-
value above 2, pH 9, 25C, R391A mutant
0.014
-
8-Amino-7-oxononanoate
-
-
0.025
-
8-Amino-7-oxononanoate
-
native enzyme
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
0.002
-
amiclenomycin
-
native enzyme
0.012
-
amiclenomycin
-
; pH 8.6, 37C
additional information
-
additional information
-
inactivation kinetics
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.057
-
3-(4-aminocyclopent-2-en-1-yl)propan-1-ol
-
pH 8.6, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
-
-
additional information
-
-
-
additional information
-
-
bioindicator assay method, overview
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
-
-
assay at
9
-
-, P12995
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
-
assay at
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
50
-
25C: about 65% of activity maximum, 50C: about 60% of activity maximum
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-, B0F481
; mitochondrial matrix
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
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)
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)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
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)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24000
-
-
sedimentation equilibrium method
94000
-
-
gel filtration, sucrose density gradient sedimentation
189000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-, B0F481
x * 90000, SDS-PAGE
dimer
-
2 * 47000, SDS-PAGE
tetramer
-
4 * 45000, SDS-PAGE
dimer
-
homodimer, crystallographic data
additional information
-, B0F481
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 ACCESSION NO.
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
-, B0F481
complex of holoenzyme and 7-keto-8-aminopelargonic acid
-
hanging drop vapor diffusion method
-
purified recombinant mutant enzymes Y17F, Y144F, D147N, R253A, and R253K, hanging drop method, 20C, 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
-, P12995
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
P9WQ80
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
11
-
30 min, stable
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7
60
-
10 min, stable
70
-
-
10 min, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, 20% glycerol, stable for 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
recombinant enzyme from strain BL21(DE3)
-
recombinant soluble N-terminally His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
; expression in Escherichia coli as truncated protein, with an N-terminal 22-residue deletion
-, B0F481
expression in strain PY79
-
cloning from strain JM101, overexpression in strain BL21(DE3)
-
overexpression of wild-type and mutant enzymes
-, P12995
wild-type and R391A mutant
-
overexpression as mostly insoluble, N-terminally His6-tagged enzyme in Escherichia coli
-
overproduced in Escherichia coli
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
F326Y
-, B0F481
mutant improves the recombinant enzyme solubility and stability; no major impact on kinetic parameters
I793W
-, B0F481
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
-, B0F481
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
-, P12995
site-directed mutagenesis, mutation of an active site residue, inactive mutant
R253A
-, P12995
site-directed mutagenesis, altered kinetics, highly increased Km for S-adenosyl-L-methionine compared to the wild-type enzyme
R253K
-, P12995
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
R253M
-, P12995
site-directed mutagenesis, altered kinetics compared to the wild-type enzyme
R253Q
-, P12995
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
-, P12995
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
-, P12995
site-directed mutagenesis, mutation of an active site residue, highly reduced activity compared to the wild-type enzyme
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-, B0F481
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
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
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
-
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
pharmacology
-
enzyme is a potential drug target in tuberculosis treatment
analysis
Mycobacterium tuberculosis ATCC 25618
-
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; 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
-