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Information on EC 2.6.1.105 - lysine-8-amino-7-oxononanoate transaminase and Organism(s) Bacillus subtilis and UniProt Accession P53555

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EC Tree
     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.105 lysine-8-amino-7-oxononanoate transaminase
IUBMB Comments
A pyridoxal 5'-phosphate enzyme . Participates in the pathway for biotin biosynthesis. The enzyme from the bacterium Bacillus subtilis cannot use S-adenosyl-L-methionine as amino donor and catalyses an alternative reaction for the conversion of 8-amino-7-oxononanoate to 7,8-diaminononanoate (cf. EC 2.6.1.62, adenosylmethionine---8-amino-7-oxononanoate transaminase).
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Bacillus subtilis
UNIPROT: P53555
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The taxonomic range for the selected organisms is: Bacillus subtilis
The enzyme appears in selected viruses and cellular organisms
Synonyms
bioA, bioK, DAPA aminotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
DAPA aminotransferase
ambiguous
PATHWAY SOURCE
PATHWAYS
-
-
SYSTEMATIC NAME
IUBMB Comments
L-lysine:8-amino-7-oxononanoate aminotransferase
A pyridoxal 5'-phosphate enzyme [2]. Participates in the pathway for biotin biosynthesis. The enzyme from the bacterium Bacillus subtilis cannot use S-adenosyl-L-methionine as amino donor and catalyses an alternative reaction for the conversion of 8-amino-7-oxononanoate to 7,8-diaminononanoate (cf. EC 2.6.1.62, adenosylmethionine---8-amino-7-oxononanoate transaminase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-lysine + 8-amino-7-oxononanoate
(S)-2-amino-6-oxohexanoate + 7,8-diaminononanoate
show the reaction diagram
additional information
?
-
presence of substrate stabilizes the loop region of the active site
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-lysine + 8-amino-7-oxononanoate
(S)-2-amino-6-oxohexanoate + 7,8-diaminononanoate
show the reaction diagram
the enzyme participates in the pathway for biotin biosynthesis
(S)-2-amino-6-oxohexanoate i.e. L-2-aminoadipate 6-semialdehyde i.e. L-allysine
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
8-Amino-7-oxononanoate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
25
8-Amino-7-oxononanoate
pH 8.3, 37°C
2
L-lysine
pH 8.3, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme participates in the pathway for biotin biosynthesis
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
to 2.2 A resolution, by molecular replacement. The overall structure is similar to its Mycobacterium tubrculosis and Escherichia coli counterparts, EC 2.6.1.62. Unlike the counterparts, a large part of the active site, i.e. Lys143-Glu172, is completely disordered in both chains. The substrate stabilizes the loop region of the Bacillus subtilis active site
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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 (P53555), Bacillus subtilis 168 (P53555)
Manually annotated by BRENDA team
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
Bacillus subtilis (P53555), Bacillus subtilis 168 (P53555)
Manually annotated by BRENDA team