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
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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
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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
5.4.3.3 lysine 5,6-aminomutaseAdvanced search results
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results (Inhibitors
Inhibitors on EC 5.4.3.3 - lysine 5,6-aminomutase
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INHIBITOR 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
IMAGE
Hydroxyadenylcobamide
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formed during isolation by degradation of enzyme-bound cobamide, strong inhibitor, tightly bound to the protein. Incubation with cobalamin, Mg2+, a mercaptan, and pyridoxal 5'-phosphate displaces the hydroxyadenylcobamide and markedly activates the enzyme
iodoacetamide
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cobamide enzyme compound is unaffected, sulfhydryl enzyme compounds is rapidly inactivated
additional information
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during catalysis under conditions where the mutase product 3,5-diaminohexanoate is not continuously removed there is extensive cleavage of cobamamide coenzyme to free 5'-deoxyadenosine and cobalamin with concomitant inactivation of the enzyme. This inactivation is prevented by the addition of sulfhydryl protein and ATP, oxygen accelerates inactivation
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additional information
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homologues of substrate D-lysine, D-2,5-diaminopentanoic acid, 2,4-diaminobutyric acid, and D-2,3-diaminopropionic acid bind to pyridoxal 5'-phosphate as an external aldimine and elicit the 5'-deoxyadenosylcobalamin Co-C bond homolysis and the accumulations of cob(II)alamin and analogue-based radicals. The position for hydrogen atom abstraction from D-2,5-diaminopentanoic acid and 2,4-diaminobutyric acid by the 5'-deoxyadenosyl radical occurs at the carbon adjacent to the imine, resulting in overstabilized radicals by spin delocalization through the imine into the pyridine ring of pyridoxal 5'-phosphate. These radicals block the active site, inhibit the enzyme, and poise the enzyme into two distinct conformations: for even-numbered analogues, the cob(II)alamin remains proximal to and spin-coupled with the analogue-based radical in the closed state while odd-numbered analogues trigger the transition to the open state of the enzyme, inactivation mechanism, overview
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additional information
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homologues of substrate D-lysine, D-2,5-diaminopentanoic acid, 2,4-diaminobutyric acid, and D-2,3-diaminopropionic acid bind to pyridoxal 5'-phosphate as an external aldimine and elicit the 5'-deoxyadenosylcobalamin Co-C bond homolysis and the accumulations of cob(II)alamin and analogue-based radicals. The position for hydrogen atom abstraction from D-2,5-diaminopentanoic acid and 2,4-diaminobutyric acid by the 5'-deoxyadenosyl radical occurs at the carbon adjacent to the imine, resulting in overstabilized radicals by spin delocalization through the imine into the pyridine ring of pyridoxal 5'-phosphate. These radicals block the active site, inhibit the enzyme, and poise the enzyme into two distinct conformations: for even-numbered analogues, the cob(II)alamin remains proximal to and spin-coupled with the analogue-based radical in the closed state while odd-numbered analogues trigger the transition to the open state of the enzyme, inactivation mechanism, overview
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