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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Cofactor
Cofactor on EC 5.4.3.3 - lysine 5,6-aminomutase
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5'-deoxyadenosylcobalamin
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shows ability to produce highly reactive 5'-deoxyadenosyl radical in enzymatic environments
5'-deoxyadenosylcobalamin
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shows ability to produce highly reactive 5'-deoxyadenosyl radical in enzymatic environments, situated in the Rossmann domain in the crystal structure, and separated from pyridoxal 5'-phosphate
5'-deoxyadenosylcobalamin
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shows ability to produce highly reactive 5'-deoxyadenosyl radical in enzymatic environments, situated in the Rossmann domain in the crystal structure, and separated from pyridoxal-5'-phosphate
adenosylcobalamin
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Km value 6.1 mM, in presence of S-subunit of D-ornithine aminomutase, Km value 3.5 mM, in presence of ATP and S-subunit of D-ornithine aminomutase, Km value 1.9 mM
Cobalamin
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required, directly involved in the catalysis of the amino group migration
Cobalamin
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coenzyme serves as carrier of the hydrogen that is transferred
pyridoxal 5'-phosphate
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Km value 3.9 mM, in presence of S-subunit of D-ornithine aminomutase, Km value 3.0 mM, in presence of ATP and S-subunit of D-ornithine aminomutase, Km value 2.4 mM
pyridoxal 5'-phosphate
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dependent on, molecular modeling in the reaction
pyridoxal 5'-phosphate
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stabilizes high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons
pyridoxal 5'-phosphate
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stabilizes high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons, bound at the top of the TIM barrel domain and separated from 5'-deoxyadenosylcobalamin, binding site structure involving residues Tyr263, Asn299, Arg184, Arg268, Ser189, Gly187, Gln188, and Ser189, overview
pyridoxal 5'-phosphate
the protonation state of the pyridoxal 5'-phosphate cofactor has less of a role in radical-mediated chemistry compared to electrostatic interactions between the substrate and protein. Binding structure analysis and comparison with ornithine 4,5-aminomutase, EC 5.4.3.5
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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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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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additional information
lysine 5,6-aminomutase is a 5'-deoxyadenosylcobalamin and pyridoxal 5'-phosphate co-dependent radical enzyme
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additional information
lysine 5,6-aminomutase is a 5'-deoxyadenosylcobalamin and pyridoxal 5'-phosphate co-dependent radical enzyme
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additional information
lysine 5,6-aminomutase is a 5'-deoxyadenosylcobalamin and pyridoxal 5'-phosphate co-dependent radical enzyme, formation of internal aldimine with pyridoxal 5'-phosphate and pyridoxal 5'-phosphate-N-oxide
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additional information
lysine 5,6-aminomutase shows flexibility toward cofactor analogue pyridoxal 5'-phosphate-N-oxide, which can act as a functional cofactor for enzyme 5,6-LAM, kinetics and structure-function analysis, overview
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