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Enzyme Nomenclature
Information on EC 5.4.3.4 - D-lysine 5,6-aminomutase
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The expected taxonomic range for this enzyme is: Acetoanaerobium sticklandii
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EC NUMBER 
COMMENTARY 
5.4.3.4
transferred to EC 5.4.3.3
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RECOMMENDED NAME
GeneOntology No.
D-lysine 5,6-aminomutase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate
(1)
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-
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D-lysine = (2R,5S)-2,5-diaminohexanoate
(2)
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D-lysine = (2R,5S)-2,5-diaminohexanoate
radical catalytic mechanism
-
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CAS REGISTRY NUMBER
COMMENTARY
9075-70-1
-
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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 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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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
-
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
-
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
-
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
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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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
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
dependent on, molecular modeling in the reaction
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.63
D-Lysine
-
pH and temperature not specified in the publication
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LINKS TO OTHER DATABASES (specific for EC-Number 5.4.3.4)
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