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
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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
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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
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synthesis
- 5.4.3.2
- s-adenosylmethionine
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5\'-deoxyadenosyl
- epr
- pyridoxal
- l-beta-lysine
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hyperfine
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adenosylcobalamin-dependent
- formate-lyase
- subterminale
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aldimine
- pyridoxal-5'-phosphate
- adenosylcobalamin
- 5'-deoxyadenosine
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cxxxcxxc
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homolytic
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deoxyadenosyl
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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
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Cofactor
Cofactor on EC 5.4.3.2 - lysine 2,3-aminomutase
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pyridoxal 5'-phosphate
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evidence for participation of pyridoxal 5'-phosphate in a radical rearrangement, formation of an aldimine linkage between the pyridoxal 5'-phosphate and the beta-nitrogen of (3S)-3,6-diaminohexanoic acid
pyridoxal 5'-phosphate
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contains 5.5 mol of pyridoxal phosphate per mol of hexameric enzyme
pyridoxal 5'-phosphate
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enzyme contains approximately 6 molecules per hexameric enzyme
pyridoxal 5'-phosphate
the cofactor facilitates the rearrangement of a substrate radical
pyridoxal 5'-phosphate
the cofactor facilitates the rearrangement of a substrate radical
pyridoxal 5'-phosphate
the cofactor facilitates the rearrangement of a substrate radical
S-adenosyl-L-methionine
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a [4Fe-4S]+ cluster reduces a bound S-adenosyl-L-methionine (SAM) molecule, cleaving it into methionine and a 5'-deoxyadenosyl radical. This step initiates the varied chemistry catalyzed by each of the so-called radical SAM enzymes
S-adenosyl-L-methionine
dependent on, activates. Reductive cleavage of S-adenosyl-L-methionine to the 5'-deoxyadenosyl radical by enzyme LAM, mechanism, overview. S-adenosyl-L-methionine dependence in the reduction of [4Fe-4S]2+ to [4Fe-4S]1+, S-adenosyl-L-methionine is in a direct interaction with the iron-sulfur cluster
S-adenosyl-L-methionine
SAM, natural cofactor, lysine 2,3-aminomutase (LAM) is a radical S-adenosyl-L-methionine (SAM) enzyme. Enzyme 2,3-LAM utilizes radical-generating machinery comprising SAM anchored to the unique Fe2+ of a [4Fe-4S] cluster via a classical five-membered N,O chelate ring. Specific activity is 35-40 IU/mg
[4Fe-4S] cluster
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a [4Fe-4S]+ cluster reduces a bound S-adenosyl-L-methionine (SAM) molecule, cleaving it into methionine and a 5'-deoxyadenosyl radical. This step initiates the varied chemistry catalyzed by each of the so-called radical SAM enzymes
[4Fe-4S] cluster
enzyme LAM contains one [4Fe-4S] cluster ligated by three cysteine residues. S-adenosyl-L-methionine dependence in the reduction of [4Fe-4S]2+ to [4Fe-4S]1+, S-adenosyl-L-methionine is in a direct interaction with the iron-sulfur cluster
enzyme LAM does not require adenosylcobalamin. It contains pyridoxal-5'-phosphate and iron and is activated by a reducing agent and S-adenosyl-L-methionine
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additional information
S-3',4'-anhydroadenosyl-L-methionine, anSAM, development of the S-adenosyl-L-methionine surrogate, the compound is a true cofactor for lysine 2,3-aminomutase. Specific activity is 0.1 IU/mg
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