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 hide
2.6.1.62
-
RECOMMENDED NAME
GeneOntology No.
adenosylmethionine-8-amino-7-oxononanoate transaminase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
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
COMMENTARY hide
LITERATURE
amino group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
biotin biosynthesis
-
-
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.
CAS REGISTRY NUMBER
COMMENTARY hide
37259-71-5
-
ORGANISM
COMMENTARY hide
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
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
NRRL 2311
-
-
Manually annotated by BRENDA team
AKV 0015
-
-
Manually annotated by BRENDA team
IFO 3764
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
-
?
DL-lysine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
show the reaction diagram
-
L-lysine is preferred
-
-
?
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
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
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-amino-8-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-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
S-adenosyl-L-methionine + 8-amino-7-oxononanoate
S-adenosyl-4-methylthio-2-oxobutanoate + 7,8-diaminononanoate
show the reaction diagram
S-adenosyl-L-methionine + sinefungin
S-adenosyl-4-methylthio-2-oxobutanoate + ?
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
DL-lysine + 8-amino-7-oxononanoate
? + (7S,8R)-diaminononanoate
show the reaction diagram
-
L-lysine is preferred
-
-
?
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 + 7,8-diaminononanoate
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
pyridoxamine 5'-phosphate
S-adenosyl-L-methionine
-
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
7-Keto-8-aminopelargonic acid
8-Amino-7-oxononanoate
8-amino-7-oxooctanoate
-
potent inhibitor
8-amino-7-oxooctanoic acid
-
achiral analog of 8-amino-7-oxononanoate
8-amino-7-oxopelargonic acid
-
;
adenine
-
8 mM
adenosine
amiclenomycin
cis-amiclenomycin
-
and analogues, overview, irreversible inactivation, kinact. 0.4 min-1, little or no inhibition by the trans-compound, overview
DL-Penicillamine
-
-
hydroxylamine
Isoniazid
p-chloromercuribenzoate
phenylhydrazine
S-Adenosyl-L-(2-hydroxy-4-methylthio)butyric acid
S-adenosyl-L-ethionine
S-adenosyl-L-homocysteine
-
5 mM
S-Inosyl-L-(2-hydroxy-4-methylthio)butyric acid
-
2 mM
Semicarbazide
additional information
-
no inhibition by the (R,S)-diastereomer of S-adenosyl-L-methionine
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001 - 1.1
7-amino-8-oxononanoate
0.0006 - 0.23
8-Amino-7-oxononanoate
0.00083 - 0.032
pyridoxal 5'-phosphate
0.0012 - 0.021
pyridoxamine 5'-phosphate
0.1 - 0.75
S-adenosyl-(5')-3-methylthiopropylamine
0.0002 - 3
S-adenosyl-L-methionine
0.7
sinefungin
pH 7.5, temperature not specified in the publication
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0021 - 1.7
8-Amino-7-oxononanoate
0.016
S-adenosyl-(5')-3-methylthiopropylamine
Escherichia coli
P12995
pH 9.0, recombinant wild-type enzyme and mutant R253K
0.001 - 0.13
S-adenosyl-L-methionine
0.009
sinefungin
Mycobacterium tuberculosis
P9WQ80
pH 7.5, temperature not specified in the publication
additional information
additional information
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
S-adenosyl-L-methionine
Mycobacterium tuberculosis
P9WQ80
pH 7.5, temperature not specified in the publication
24
0.013
sinefungin
Mycobacterium tuberculosis
P9WQ80
pH 7.5, temperature not specified in the publication
659
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0017 - 0.0059
(R)-8-amino-7-oxononanoate
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 - 0.02
3-(cis-4-aminocyclohexa-2,5-dien-1-yl)propan-1-ol
0.025 - 2
7-Keto-8-aminopelargonic acid
0.014 - 0.025
8-Amino-7-oxononanoate
0.0009 - 0.0042
8-amino-7-oxooctanoate
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 - 0.012
amiclenomycin
additional information
additional information
-
inactivation kinetics
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.057
3-(4-aminocyclopent-2-en-1-yl)propan-1-ol
Mycobacterium tuberculosis
-
pH 8.6, 25C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 50
-
25C: about 65% of activity maximum, 50C: about 60% of activity maximum
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
; mitochondrial matrix
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
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 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)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24000
-
sedimentation equilibrium method
94000
-
gel filtration, sucrose density gradient sedimentation
189000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 90000, SDS-PAGE
tetramer
-
4 * 45000, SDS-PAGE
additional information
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
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 11
-
30 min, stable
1335, 637090
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 60
-
10 min, stable
70
-
10 min, complete loss of activity
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20% glycerol, stable for 1 year
-
Purification/COMMENTARY
ORGANISM
UNIPROT
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
LITERATURE
; expression in Escherichia coli as truncated protein, with an N-terminal 22-residue deletion
cloning from strain JM101, overexpression in strain BL21(DE3)
-
expression in strain PY79
-
overexpression as mostly insoluble, N-terminally His6-tagged enzyme in Escherichia coli
-
overexpression of wild-type and mutant enzymes
overproduced in Escherichia coli
-
wild-type and R391A mutant
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
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
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