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Literature summary extracted from

  • Sandmark, J.; Eliot, A.C.; Famm, K.; Schneider, G.; Kirsch, J.F.
    Conserved and nonconserved residues in the substrate binding site of 7,8-diaminopelargonic acid synthase from Escherichia coli are essential for catalysis (2004), Biochemistry, 43, 1213-1222.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.6.1.62 overexpression of wild-type and mutant enzymes Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.6.1.62 purified recombinant mutant enzymes Y17F, Y144F, D147N, R253A, and R253K, hanging drop method, 20°C, 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 Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.6.1.62 D147N site-directed mutagenesis, mutation of an active site residue, inactive mutant Escherichia coli
2.6.1.62 R253A site-directed mutagenesis, altered kinetics, highly increased Km for S-adenosyl-L-methionine compared to the wild-type enzyme Escherichia coli
2.6.1.62 R253K site-directed mutagenesis, altered kinetics compared to the wild-type enzyme Escherichia coli
2.6.1.62 R253M site-directed mutagenesis, altered kinetics compared to the wild-type enzyme Escherichia coli
2.6.1.62 R253Q site-directed mutagenesis, altered kinetics compared to the wild-type enzyme Escherichia coli
2.6.1.62 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 Escherichia coli
2.6.1.62 Y17F site-directed mutagenesis, mutation of an active site residue, highly reduced activity compared to the wild-type enzyme Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.6.1.62 additional information
-
 additional information single turnover reactions, stopped-flow, wild-type and mutant enzymes Escherichia coli
2.6.1.62 0.0006
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant R253M Escherichia coli
2.6.1.62 0.0008
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant R253K Escherichia coli
2.6.1.62 0.001
-
 8-Amino-7-oxononanoate pH 9.0, recombinant wild-type enzyme Escherichia coli
2.6.1.62 0.0014
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant R253Q Escherichia coli
2.6.1.62 0.0022
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant R253A Escherichia coli
2.6.1.62 0.01
-
 S-adenosyl-L-methionine pH 9.0, recombinant mutant R253K Escherichia coli
2.6.1.62 0.011
-
 S-adenosyl-L-methionine pH 9.0, recombinant mutant R253Q Escherichia coli
2.6.1.62 0.02
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant Y17F Escherichia coli
2.6.1.62 0.063
-
 S-adenosyl-L-methionine pH 9.0, recombinant mutant Y17F Escherichia coli
2.6.1.62 0.1
-
 S-adenosyl-(5')-3-methylthiopropylamine pH 9.0, recombinant mutant R253K Escherichia coli
2.6.1.62 0.15
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant Y144F Escherichia coli
2.6.1.62 0.3
-
 S-adenosyl-L-methionine pH 9.0, recombinant wild-type enzyme Escherichia coli
2.6.1.62 0.75
-
 S-adenosyl-(5')-3-methylthiopropylamine pH 9.0, recombinant wild-type enzyme Escherichia coli
2.6.1.62 1
-
 S-adenosyl-L-methionine pH 9.0, recombinant mutant R253A Escherichia coli
2.6.1.62 3
-
 S-adenosyl-L-methionine pH 9.0, recombinant mutant Y144F Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.6.1.62 S-adenosyl-L-methionine + 8-amino-7-oxononanoate Escherichia coli second of 4 steps in the biosynthesis of vitamin H, i.e. biotin S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
 r

Organism

EC Number Organism UniProt Comment Textmining
2.6.1.62 Escherichia coli P12995
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.6.1.62 S-adenosyl-L-methionine + 8-amino-7-oxononanoate = S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate + 7,8-diaminononanoate reaction mechanism, substrate binding structure, detailed reversible aminotransferase half-reaction, overview, residues Tyr17, Asp147, and conserved Tyr144 and Arg253 are important for catalysis Escherichia coli
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.6.1.62 S-adenosyl-(5')-3-methylthiopropylamine + 8-amino-7-oxononanoate decarboxylated S-adenosyl-L-methionine is as reactive as S-adenosyl-L-methionine Escherichia coli ? + (7S,8R)-diaminononanoate
-
 r
2.6.1.62 S-adenosyl-L-methionine + 8-amino-7-oxononanoate second of 4 steps in the biosynthesis of vitamin H, i.e. biotin Escherichia coli S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
 r
2.6.1.62 S-adenosyl-L-methionine + 8-amino-7-oxononanoate the aminotransferase half-reaction is reversible, substrate binding structure Escherichia coli S-adenosyl-4-methylthio-2-oxobutanoate + (7S,8R)-diaminononanoate
-
 r

Synonyms

EC Number Synonyms Comment Organism
2.6.1.62 7,8-diaminopelargonic acid synthase
-
 Escherichia coli
2.6.1.62 DAPA synthase
-
 Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.6.1.62 additional information
-
 additional information single turnover reactions Escherichia coli
2.6.1.62 0.001
-
 S-adenosyl-L-methionine pH 9.0, recombinant mutant R253A Escherichia coli
2.6.1.62 0.0035
-
 S-adenosyl-L-methionine pH 9.0, recombinant mutant Y17F Escherichia coli
2.6.1.62 0.009
-
 S-adenosyl-L-methionine pH 9.0, recombinant mutant R253K Escherichia coli
2.6.1.62 0.01
-
 S-adenosyl-L-methionine pH 9.0, recombinant mutant R253M Escherichia coli
2.6.1.62 0.012
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant Y17F Escherichia coli
2.6.1.62 0.016
-
 S-adenosyl-L-methionine pH 9.0, recombinant wild-type enzyme Escherichia coli
2.6.1.62 0.016
-
 S-adenosyl-(5')-3-methylthiopropylamine pH 9.0, recombinant wild-type enzyme and mutant R253K Escherichia coli
2.6.1.62 0.04
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant Y144F Escherichia coli
2.6.1.62 0.06
-
 S-adenosyl-L-methionine pH 9.0, recombinant mutant Y144F Escherichia coli
2.6.1.62 0.074
-
 S-adenosyl-L-methionine pH 9.0, recombinant mutant R253Q Escherichia coli
2.6.1.62 0.67
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant R253M Escherichia coli
2.6.1.62 0.79
-
 8-Amino-7-oxononanoate pH 9.0, recombinant wild-type enzyme Escherichia coli
2.6.1.62 1.3
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant R253A Escherichia coli
2.6.1.62 1.3
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant R253K Escherichia coli
2.6.1.62 1.7
-
 8-Amino-7-oxononanoate pH 9.0, recombinant mutant R253Q Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.6.1.62 9
-
 assay at Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.6.1.62 pyridoxal 5'-phosphate i.e. vitamin B6, dependent on Escherichia coli