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
Advanced search results
Metals Ions
Metals Ions 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.
Co2+
Cu2+
-
enzyme-bound, occupies cobalt sites in the enzyme under conditions of insufficient cobalt in the growth medium, even the best preparations contain a small amount
Fe
contains traces of iron, and activity is enhanced by addition of ferrous ions
Fe2+
Iron
Zn2+
Fe2+
-
the activity is modestly increased by the addition of ferrous iron
Fe2+
one [4Fe-4S] cluster, the iron-binding motif in LAM is CxxxCxxC
Iron
-
[4Fe-4S] cluster. Reduction potential for the cluster is lowered by 0.17 V by the binding of lysine to enzyme, and the binding of S-adenosyl-L-methionine to the cluster elevates its reduction potential by 0.81 V. Thus binding of L-lysine and S-adenosylmethionine lower the barrier for reductive cleavage of S-adenosylmethionine at the active site from 32 kcal per mol to 9 kcal per mol
Iron
-
[4Fe-4S]2+/1+ couple shows midpoint reduction potentials of -430 mV in presence of S-adenosyl-L-methionine, -460 mV in presence of S-adenosyl-l-homocysteine, -497 mV in presence of 5-(N-[(3S)-3-aminocarboxypropyl]-N-methylamino)-5-deoxyadenosine. In presence of dithiothreitol, dihydrolipoate, or cysteine, midpoint potentials are -479, -516, and -484 mV, resp.
-
enzyme-bound, occupies cobalt sites in the enzyme under conditions of insufficient cobalt in the growth medium, even the best preparations contain a small amount
Zn2+
activates, the enzyme contains a zinc binding site
Zn2+
activates, the enzyme contains a zinc binding site