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Literature summary for 5.4.3.3 extracted from

  • Makins, C.; Whitelaw, D.A.; McGregor, M.; Petit, A.; Mothersole, R.G.; Prosser, K.E.; Wolthers, K.R.
    Optimal electrostatic interactions between substrate and protein are essential for radical chemistry in ornithine 4,5-aminomutase (2017), Biochim. Biophys. Acta, 1865, 1077-1084 .
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
genes FN1863 and FN1862 encoding the alpha- and beta-subunit, respectively, recombinant expression in Escherichia coli strain Rosetta(DE3) pLysS Fusobacterium nucleatum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(3S)-3,6-diaminohexanoate Fusobacterium nucleatum
-
(3S,5S)-3,5-diaminohexanoate
-
r
D-lysine Fusobacterium nucleatum
-
2,5-diaminohexanoate
-
r

Organism

Organism UniProt Comment Textmining
Fusobacterium nucleatum Q8RHX7 AND Q8RHX8 alpha- and beta-subunits
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(3S)-3,6-diaminohexanoate
-
Fusobacterium nucleatum (3S,5S)-3,5-diaminohexanoate
-
r
D-lysine
-
Fusobacterium nucleatum 2,5-diaminohexanoate
-
r
additional information 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 Fusobacterium nucleatum ?
-
?

Subunits

Subunits Comment Organism
heterotetramer alpha2beta2 Fusobacterium nucleatum

Synonyms

Synonyms Comment Organism
LAM
-
Fusobacterium nucleatum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
25
-
assay at Fusobacterium nucleatum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8.5
-
assay at Fusobacterium nucleatum

Cofactor

Cofactor Comment Organism Structure
5'-deoxyadenosylcobalamin
-
Fusobacterium nucleatum
additional information lysine 5,6-aminomutase is a 5'-deoxyadenosylcobalamin and pyridoxal 5'-phosphate co-dependent radical enzyme Fusobacterium nucleatum
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 Fusobacterium nucleatum

General Information

General Information Comment Organism
additional information lysine 5,6-aminomutase (5,6-LAM) from Clostridium sticklandii is an adenosylcobalamin (AdoCbl) and pyridoxal 5'-phosphate (PLP)-dependent enzyme Fusobacterium nucleatum