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
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5.4.3.2
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s-adenosylmethionine
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5\'-deoxyadenosyl
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epr
-
pyridoxal
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l-beta-lysine
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hyperfine
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adenosylcobalamin-dependent
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formate-lyase
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subterminale
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aldimine
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pyridoxal-5'-phosphate
-
adenosylcobalamin
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5'-deoxyadenosine
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cxxxcxxc
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homolytic
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deoxyadenosyl
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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
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Systematic Name
Systematic Name on EC 5.4.3.2 - lysine 2,3-aminomutase
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L-lysine 2,3-aminomutase
This enzyme is a member of the 'AdoMet radical' (radical SAM) family. It contains pyridoxal phosphate and a [4Fe-4S] cluster and binds an exchangeable S-adenosyl-L-methionine molecule. Activity in vitro requires a strong reductant such as dithionite and strictly anaerobic conditions. A 5'-deoxyadenosyl radical is generated during the reaction cycle by reductive cleavage of S-adenosyl-L-methionine, mediated by the iron-sulfur cluster. S-adenosyl-L-methionine is regenerated at the end of the reaction.