5.4.3.2: lysine 2,3-aminomutase
This is an abbreviated version!
For detailed information about lysine 2,3-aminomutase, go to the full flat file.
Word Map on EC 5.4.3.2
-
5.4.3.2
-
s-adenosylmethionine
-
5\'-deoxyadenosyl
-
epr
-
pyridoxal
-
l-beta-lysine
-
hyperfine
-
adenosylcobalamin-dependent
-
formate-lyase
-
subterminale
-
aldimine
-
pyridoxal-5'-phosphate
-
adenosylcobalamin
-
5'-deoxyadenosine
-
cxxxcxxc
-
homolytic
-
deoxyadenosyl
-
aminomutases
-
synthesis
- 5.4.3.2
- s-adenosylmethionine
-
5\'-deoxyadenosyl
- epr
- pyridoxal
- l-beta-lysine
-
hyperfine
-
adenosylcobalamin-dependent
- formate-lyase
- subterminale
-
aldimine
- pyridoxal-5'-phosphate
- adenosylcobalamin
- 5'-deoxyadenosine
-
cxxxcxxc
-
homolytic
-
deoxyadenosyl
-
aminomutases
- synthesis
Reaction
Synonyms
AblA, Aminomutase, lysine 2,3-, HD73_2540, KAM, kamA, L-Lysine-2,3-aminomutase, LAM, lysine 2,3-aminomutase, lysine-2,3-aminomutase, Mutase, lysine 2,3-amino-, YjeK
ECTree
5.4.3.2 lysine 2,3-aminomutaseAdvanced search results
results (
results (Activating Compound
Activating Compound on EC 5.4.3.2 - lysine 2,3-aminomutase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
ACTIVATING COMPOUND 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Dithionite
activity absolutely depends on the addition of dithionite
ethylamine
-
saturating ethylamine accelerates the L-alanine reaction 70fold
Ferredoxin
-
enzyme activity is dependent on the presence of flavodoxin, ferredoxin, or flavodoxin-NADP+ reductase
-
flavodoxin
-
enzyme activity is dependent on the presence of flavodoxin, ferredoxin, or flavodoxin-NADP+ reductase
-
methylamine
-
saturating methylamine accelerates the L-2-aminobutyrate reaction 47fold
sulfhydryl compound
-
can reactivate oxygen-inactivated enzyme, optimal activation when 0.9 mM Fe2+ is present
S-adenosyl-L-methionine
functions as a hydrogen transfer agent in this aminomutase reaction
S-adenosyl-L-methionine
functions as a hydrogen transfer agent in this aminomutase reaction
S-adenosyl-L-methionine
functions as a hydrogen transfer agent in this aminomutase reaction
S-adenosylmethionine
-
activation of the enzyme involves a transfer of the 5'-deoxyadenosyl moiety from S-adenosylmethionine to another species associated with the enzyme, presumably another cofactor, to form an adenosyl cofactor that functions as the proximal, hydrogen abstracting species
S-adenosylmethionine
-
the 5'-deoxyadenosyl moiety of S-adenosylmethionine mediates hydrogen transfer
S-adenosylmethionine
-
does not serve as hydrogen carrier in the reaction
S-adenosylmethionine
-
plays a role in lysine 2,3-aminomutase reaction
S-adenosylmethionine
activity absolutely depends on the addition of S-adenosylmethionine
