5.4.3.3: lysine 5,6-aminomutase
This is an abbreviated version!
For detailed information about lysine 5,6-aminomutase, go to the full flat file.
Word Map on EC 5.4.3.3
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5.4.3.3
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adenosylcobalamin
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pyridoxal-5'-phosphate
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paramagnetic
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sticklandii
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pyridoxal
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cobiialamin
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adenosylcobalamin-dependent
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homolysis
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5\'-deoxyadenosyl
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5'-phosphate
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4,5-aminomutase
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5\'-deoxyadenosylcobalamin
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aldimine
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l-beta-lysine
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d-ornithine
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pyridoxal-5'-phosphate-dependent
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substrate-related
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dl-lysine
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1,2-amino
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cobalamin-dependent
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adocbl
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plp-binding
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adenosyl
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5'-deoxyadenosine
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plp-dependent
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transaldimination
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spin-coupled
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cobalamin-binding
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hyperfine
- 5.4.3.3
- adenosylcobalamin
- pyridoxal-5'-phosphate
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paramagnetic
- sticklandii
- pyridoxal
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cobiialamin
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adenosylcobalamin-dependent
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homolysis
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5\'-deoxyadenosyl
- 5'-phosphate
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4,5-aminomutase
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5\'-deoxyadenosylcobalamin
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aldimine
- l-beta-lysine
- d-ornithine
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pyridoxal-5'-phosphate-dependent
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substrate-related
- dl-lysine
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1,2-amino
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cobalamin-dependent
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adocbl
-
plp-binding
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adenosyl
- 5'-deoxyadenosine
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plp-dependent
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transaldimination
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spin-coupled
-
cobalamin-binding
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hyperfine
Reaction
Synonyms
(R)-lysine mutase, 5,6-LAM, beta-Lysine mutase, EC 5.4.3.4, KamDE, LAM, lysine 5,6-aminomutase
ECTree
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D298A
site-directed mutagenesis, the mutation of the alpha-subunit
D298N
site-directed mutagenesis, the mutation of the alpha-subunit reduces the enzymatic activity in converting D-lysine into D-2,5-diaminohexanoic acid
K370A
site-directed mutagenesis, the mutation of the alpha-subunit reduces the enzymatic activity in converting D-lysine into D-2,5-diaminohexanoic acid
K370Q
site-directed mutagenesis, the mutation of the alpha-subunit reduces the enzymatic activity in converting D-lysine into D-2,5-diaminohexanoic acid
additional information
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protein KamDE comprised of the 30000 and 51000 kDa subunits of the E1 component of D-alpha-lysine aminomutase is catalytically active in absence of the third 12800 kDa subunit, but ATP no longer has a regulatory effect on it. The S subunit of D-ornithine aminomutase, OraS, is capable of forming a complex with KamDE and restores the enzymes ATP-dependent allosteric regulation. OraS protein alone lowers the Km of KamDE for adenosylcobalamin and pyridoxal phosphate
