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 (Substrates Products
Substrates Products on EC 5.4.3.3 - lysine 5,6-aminomutase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-thia-(R)-lysine
?
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4-thia-(R)-lysine reacts with the complex of pyridoxal 5'-phosphate, adenosylcobalamin, and lysine 5,6-aminomutase to generate cob(II)alamin, 5'-deoxyadenosine, and 4-thialysine-based free radicals
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?
4-thia-(S)-lysine
?
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4-thia-(S)-lysine reacts with the complex of pyridoxal 5'-phosphate, adenosylcobalamin, and lysine 5,6-aminomutase to generate cob(II)alamin, 5'-deoxyadenosine, and 4-thialysine-based free radicals
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-
?
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
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-
-
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r
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
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-
-
r
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
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-
-
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r
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
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-
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r
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
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-
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?
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
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5,6-LAM has both beta-lysine 5,6-aminomutase and D-lysine 5,6-aminomutase activity
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?
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
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-
-
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r
(3S)-3,6-diaminohexanoate
(3S,5S)-3,5-diaminohexanoate
Propionibacterium freudenreichii ATCC 9614
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-
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r
3,6-Diaminohexanoate
3,5-Diaminohexanoate
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-
(3S,5S)-3,5-diaminohexanoate
?
3,6-Diaminohexanoate
3,5-Diaminohexanoate
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(3S)-beta-lysine
(3S,5S)-3,5-diaminohexanoate
?
D-lysine
2,5-diaminohexanoate
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equilibrium constant of 1.2
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?
L-lysine
2,5-diaminohexanoate
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first step in D-lysine catabolism
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r
additional information
?
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5-fluorolysine as substrate binding in the active site: computational simulations, the enzyme 5,6-LAM abstracts the hydrogen atom rather than the fluorine at C5 of 5-fluorolysine and subsequent rearrangement mimicking the similar mechanism as the natural substrate of the enzyme
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-
?
additional information
?
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the enzyme can accept D-lysine and L-beta-lysine
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-
?
additional information
?
-
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the enzyme can accept D-lysine and L-beta-lysine
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-
?
additional information
?
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the enzyme can accept D-lysine and L-beta-lysine. The enzyme employs radical generating capability of coenzyme B12, i.e. 5'-deoxyadenosylcobalamin, and ability of pyridoxal 5'-phosphate, i.e. vitamin B6, to stabilize high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons
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-
?
additional information
?
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-
the enzyme can accept D-lysine, L-lysine, and L-beta-lysine. The enzyme employs radical generating capability of coenzyme B12, i.e. 5'-deoxyadenosylcobalamin, and ability of pyridoxal-5'-phosphate, i.e.vitamin B6, to stabilize high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons
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?
additional information
?
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lysine 5,6-aminomutase, 5,6-LAM, catalyzes the reversible amino shift between C6 and C5 of D-lysine and L-beta-lysine. 5,6-LAM is a 5'-deoxyadenosylcobalamin and pyridoxal 5'-phosphate co-dependent radical enzyme, molecular mechanism of the open-closed protein conformational cycle transitions and coupled substrate binding, activation and product release events in lysine 5,6-aminomutase, overview
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?
additional information
?
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the enzyme can accept D-lysine and L-beta-lysine
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?
additional information
?
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lysine 5,6-aminomutase (5,6-LAM) can perform 1,2-amino shifts on L-beta-lysine as well as D- and L-lysine. Docking of L-lysine or L-beta-lysine into the active site of 5,6-LAM revealed distinct non-covalent interactions between the substrate and the enzyme compared to that of the ornithine 4,5-aminomutase (EC 5.4.3.5) substrate complex. In 5,6-LAM, K370alpha forms a salt bridge with the alpha-carboxylate of the lysyl-pyridoxal 5'-phosphate complex, while the alpha-amine interacts with D298alpha. These two substitutions presumably increase the binding cavity of 5,6-LAM to accommodate different isomers of lysine. 5,6-LAM is able to act on D-lysine
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?
additional information
?
-
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the enzyme can accept D-lysine and L-beta-lysine. The enzyme employs radical generating capability of coenzyme B12, i.e. 5'-deoxyadenosylcobalamin, and ability of pyridoxal 5'-phosphate, i.e. vitamin B6, to stabilize high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons
-
-
?
additional information
?
-
-
the enzyme can accept D-lysine and L-beta-lysine. The enzyme employs radical generating capability of coenzyme B12, i.e. 5'-deoxyadenosylcobalamin, and ability of pyridoxal 5'-phosphate, i.e.vitamin B6, to stabilize high-energy intermediates for performing challenging 1,2-amino rearrangements between adjacent carbons
-
-
?
additional information
?
-
-
the enzyme can accept D-lysine and L-beta-lysine
-
-
?
additional information
?
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Propionibacterium freudenreichii ATCC 9614
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the enzyme can accept D-lysine and L-beta-lysine
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-
?
