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
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General Information on EC 5.4.3.3 - lysine 5,6-aminomutase
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GENERAL INFORMATION 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
evolution
malfunction
the D298N, D298A, K370Q, and K370A variants of the alpha-subunits abolish the enzymatic activity in converting D-lysine into D-2,5-diaminohexanoic acid
metabolism
additional information
evolution
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the enzyme belongs to the class III dAdoCbl-dependent isomerase family
evolution
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the enzyme belongs to the class III dAdoCbl-dependent isomerase family
metabolism
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lysine 5,6-aminomutase is essential for the metabolism of L- or D-lysine in anaerobic bacteria
metabolism
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lysine 5,6-aminomutase participates in the fermentation of L- or D-lysine as carbon and nitrogen sources in anaerobic bacteria
metabolism
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the enzyme participates in the second step of the fermentation pathway of lysine in which lysine is converted to acetic acid, ammonia and butyric acid
metabolism
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the enzyme participates in the second step of the fermentation pathway of lysine in which lysine is converted to acetic acid, ammonia and butyric acid
additional information
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a large-scale domain movement is required for interconversion between the catalytically inactive open form and the catalytically active closed form. The recombinant enzyme (KamDE) containing only E1 is active, but is subjected to suicide inactivation with the substrate
additional information
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active site structure, overview. A large-scale domain movement is required for interconversion between the catalytically inactive open form and the catalytically active closed form. The recombinant enzyme (KamDE) containing only E1 is active, but is subjected to suicide inactivation with the substrate. Modeling of the closed conformation of the enzyme, domain motions, overview
additional information
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the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine
additional information
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the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine
additional information
both Asp298alpha and Lys370alpha are functionally important residues in enzyme 5,6-LAM
additional information
lysine 5,6-aminomutase (5,6-LAM) from Clostridium sticklandii is an adenosylcobalamin (AdoCbl) and pyridoxal 5'-phosphate (PLP)-dependent enzyme
additional information
Propionibacterium freudenreichii ATCC 9614
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the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine
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additional information
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the closed-state of the enzyme is required to bring the cofactors adenosylcobalamin and pyridoxal 5'-phosphate and the substrate into proximity for the radical-mediated 1,2-amino group migration. This process is achieved by transaldimination of the pyridoxal 5'-phosphate-Lys144beta internal aldimine with the pyridoxal 5'-phosphate-substrate external aldimine
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