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2.6.1.62: adenosylmethionine-8-amino-7-oxononanoate transaminase

This is an abbreviated version!
For detailed information about adenosylmethionine-8-amino-7-oxononanoate transaminase, go to the full flat file.

Word Map on EC 2.6.1.62

Reaction

S-adenosyl-L-methionine
+
8-Amino-7-oxononanoate
=
S-adenosyl-4-(methylsulfanyl)-2-oxobutanoate
+
7,8-diaminononanoate

Synonyms

7,8-diaminononanoate transaminase, 7,8-diaminopelargonate synthase, 7,8-diaminopelargonic acid aminotransferase, 7,8-diaminopelargonic acid synthase, 7,8-diaminopelargonic acid transaminase, 7,8-diaminoperlargonic acid aminotransferase, 7-keto-8-aminopelargonic acid aminotransferase, 7-keto-8-aminopelargonic acid-7,8-diaminopelargonic acid aminotransferase, Bio3-Bio1, bioA, DAPA amino transferase, DAPA aminotransferase, DAPA AT, DAPA synthase, DAPA transaminase, diaminopelargonate synthase, diaminopelargonic acid transaminase, diaminoperlargonic acid aminotransferase, More, NCgl2515, Pcryo_0361, S-adenosyl-L-methionine:8-amino-7-oxononanoate aminotransferase, synthase, diaminopelargonate

ECTree

     2 Transferases
         2.6 Transferring nitrogenous groups
             2.6.1 Transaminases
                2.6.1.62 adenosylmethionine-8-amino-7-oxononanoate transaminase

Engineering

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

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F326Y
I793W
S360Y
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
additional information