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Information on EC 2.6.1.17 - succinyldiaminopimelate transaminase for references in articles please use BRENDA:EC2.6.1.17
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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
aminotransferase, succinyldiaminopimelate, AspB2, DAP-AT, DapC, N-succinyl-L-diaminopimelic-glutamic transaminase, Rv0858c, SDAT-AT, succinyldiaminopimelate aminotransferase,
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aminotransferase, succinyldiaminopimelate
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N-succinyl-L-diaminopimelic-glutamic transaminase
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succinyldiaminopimelate aminotransferase
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AspB2
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DAP-AT
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DapC
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N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate = N-succinyl-L-2-amino-6-oxoheptanedioate + L-glutamate
A pyridoxal-phosphate protein
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amino group transfer
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N-succinyl-L-2,6-diaminoheptanedioate:2-oxoglutarate aminotransferase
A pyridoxal-phosphate protein.
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
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?
prephenate + N-succinyl-L-2,6-diaminoheptanedioate
L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate
additional information
?
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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i.e. N-succinyl-alpha-amino-epsilon-ketopimelic acid
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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completely specific towards L-glutamate
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r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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a key enzyme in the bacterial pathway to L-lysine
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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r
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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?
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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r
prephenate + N-succinyl-L-2,6-diaminoheptanedioate
L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate
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prephenate + N-succinyl-L-2,6-diaminoheptanedioate
L-arogenate + N-succinyl-2-amino-6-oxoheptanedioate
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additional information
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structural requirements for substrate recognition
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additional information
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enzyme is not identical to N-acetylornithine aminotransferase
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additional information
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enzyme is not identical to N-acetylornithine aminotransferase
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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a key enzyme in the bacterial pathway to L-lysine
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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N-succinyl-2-amino-6-oxoheptanedioate + L-glutamate
N-succinyl-L-2,6-diaminoheptanedioate + 2-oxoglutarate
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pyridoxal 5'-phosphate
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a pyridoxal phosphate protein
pyridoxal 5'-phosphate
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2-(N-(succinylamino))-6-hydrazinoheptane-1,7-dioic acid
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very potent slow-binding inhibitor, synthesis
2-(N-Carbobenzoxy-amino)-6-hydrazinoheptane-1,7-dioic acid
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very potent slow-binding inhibitor, synthesis
2-oxoglutarate
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at high concentrations, inhibition in both directions
additional information
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synthesis of hydrazino product analogues which are potent slow tight-binding inhibitors, kinetics
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0.18 - 0.5
N-Succinyl-2-amino-6-oxoheptanedioate
0.021
prephenate
pH 8.0, 30°C
1.21
L-glutamate
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30°C, pH 8.0
0.18
N-Succinyl-2-amino-6-oxoheptanedioate
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30°C, pH 8.0
0.5
N-Succinyl-2-amino-6-oxoheptanedioate
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pH 7.4
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prephenate
pH 8.0, 30°C
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0.000004
2-(N-(succinylamino))-6-hydrazinoheptane-1,7-dioic acid
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30°C, pH 8.0
0.000054
2-(N-Carbobenzoxy-amino)-6-hydrazinoheptane-1,7-dioic acid
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30°C, pH 8.0
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8
assay at
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6.5 - 9
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pH 6.5: about 25% of maximum activity, pH 9: about 60% of maximum activity
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SwissProt
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SwissProt
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Uniprot
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Uniprot
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no activity in Brewer's yeast
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no activity in Lactobacillus casei
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no activity in Streptococcus sp.
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no activity in Sus scrofa
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bifunctional diaminopimelate aminotransferase and aspartate:prephenate aminotransferase, EC 2.6.1.79
UniProt
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bifunctional diaminopimelate aminotransferase and aspartate:prephenate aminotransferase, EC 2.6.1.79
UniProt
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physiological function
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in Escherichia coli, the major enzymes with N-succinyl-L,L-diaminopimelate aminotransferase (SDAP-AT) activity in lysine synthesis are ArgD, AstC, and SerC. Lysine availability does not regulate synthesis of the major SDAP-ATs. Complementation analysis of mutants lacking aminotransferases shows that the SDAP-ATs and alanine aminotransferases are exceptionally redundant, and this redundancy may ensure peptidoglycan synthesis
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Aspergillus kawachii (strain NBRC 4308)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Aspergillus kawachii (strain NBRC 4308)
Aspergillus kawachii (strain NBRC 4308)
Aspergillus kawachii (strain NBRC 4308)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)
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39900
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2 * 39900, SDS-PAGE, MALDI-TOF mass spectra
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homodimer
x-ray crystallography
additional information
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contains multiple imperfect-hexapeptide-repeat units
dimer
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2 * 39900, SDS-PAGE, MALDI-TOF mass spectra
dimer
crystallization data
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diffration to 2.0 A resolution. The orthorhombic crystals contain one functional dimer in the asymmetric unit. The homodimer displays the typical S-shape of class I pyridoxal 5'-phosphate-binding proteins. The two active sites of the dimer both feature an internal aldimine with the co-factor pyridoxal 5'-phosphate covalently bound to the Lys232, although neither substrate nor cofactor has been added during protein production, purification and crystallization. Nine water molecules are conserved in the active site and form an intricate hydrogen-bonding network with the co-factor and the surrounding amino acid residues; sitting drop vapour diffusion method, in the presence of 20% (w/v) PEG-3350, Tris-HCl (pH 8.5) and 200 mM MgCl2
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additional information
enzyme deletion mutant, normal growth with excess carbon and limited ammonium medium
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affinity column chromatography and gel filtration
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expressed in Escherichia coli
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synthesis
overexpression of enzyme, increase in production of L-lysine, 10fold increase in enzyme activity of strain
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Vaara, M.
Eight bacterial proteins, including UDP-N-acetylglucosamine acyltransferase (LpxA) and three other transferases of Escherichia coli, consist of a six-residue periodicity theme
FEMS Microbiol. Lett.
97
249-254
1992
Escherichia coli
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brenda
Peterkofsky, B.; Gilvarg, C.
N-succinyl-L-diaminopimelic-glutamic transaminase
J. Biol. Chem.
236
1432-1438
1961
Alcaligenes faecalis, Azotobacter vinelandii, Desmonostoc muscorum, Escherichia coli, Klebsiella aerogenes, Lactobacillus plantarum, Micrococcus luteus, no activity in Brewer's yeast, no activity in Lactobacillus casei, no activity in Streptococcus sp., no activity in Sus scrofa, Rhodobacter sphaeroides
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Cox, R.J.; Sherwin, W.A.; Lam, L.K.P.; Vederas, J.C.
Synthesis and evaluation of novel substrates and inhibitors of N-succinyl-LL-diaminopimelate aminotransferase (DAP-AT) from Escherichia coli
J. Am. Chem. Soc.
118
7449-7460
1996
Escherichia coli
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Cox, R.J.; Schouten, J.A.; Stentiford, R.A.; Wareing, K.J.
Peptide inhibitors of N-succinyl diaminopimelic acid aminotransferase (DAP-AT): a novel class of antimicrobial compounds
Bioorg. Med. Chem. Lett.
8
945-950
1998
Escherichia coli
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Cox, R.J.; Wang, P.S.H.
Is N-acetylornithine aminotransferase the real N-succinyl-LL-diaminopimelate aminotransferase in Escherichia coli and Mycobacterium smegmatis?
J. Chem. Soc. Perkin Trans. I
1
2006-2008
2001
Escherichia coli, Mycolicibacterium smegmatis
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Fuchs, T.M.; Schneider, B.; Krumbach, K.; Eggeling, L.; Gross, R.
Characterization of a Bordetella pertussis diaminopimelate (DAP) biosynthesis locus identifies dapC, a novel gene coding for an N-succinyl-L,L-DAP aminotransferase
J. Bacteriol.
182
3626-3631
2000
Bordetella pertussis (Q9ZEX3)
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Hartmann, M.; Tauch, A.; Eggeling, L.; Bathe, B.; Mockel, B.; Puhler, A.; Kalinowski, J.
Identification and characterization of the last two unknown genes, dapC and dapF, in the succinylase branch of the L-lysine biosynthesis of Corynebacterium glutamicum
J. Biotechnol.
104
199-211
2003
Corynebacterium glutamicum (Q8NRE6)
brenda
Weyand, S.; Kefala, G.; Weiss, M.S.
The three-dimensional structure of N-succinyldiaminopimelate aminotransferase from Mycobacterium tuberculosis
J. Mol. Biol.
367
825-838
2007
Mycobacterium tuberculosis (P9WPZ5), Mycobacterium tuberculosis H37Rv (P9WPZ5)
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Graindorge, M.; Giustini, C.; Kraut, A.; Moyet, L.; Curien, G.; Matringe, M.
Three different classes of aminotransferases evolved prephenate aminotransferase functionality in arogenate-competent microorganisms
J. Biol. Chem.
289
3198-3208
2014
Streptomyces avermitilis (Q82IK5), Streptomyces avermitilis DSM 46492 (Q82IK5)
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Lal, P.B.; Schneider, B.L.; Vu, K.; Reitzer, L.
The redundant aminotransferases in lysine and arginine synthesis and the extent of aminotransferase redundancy in Escherichia coli
Mol. Microbiol.
94
843-856
2014
Escherichia coli
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