1.13.11.53: acireductone dioxygenase (Ni2+-requiring)

This is an abbreviated version!
For detailed information about acireductone dioxygenase (Ni2+-requiring), go to the full flat file.

Word Map on EC 1.13.11.53

Reaction

1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one
+
O2
=
3-(methylsulfanyl)propanoate
+
formate
+
CO

Synonyms

2-hydroxy-3-keto-5-thiomethylpent-1-ene dioxygenase, aci-reductone dioxygenase, acidoreductone dioxygenase, acireductone dioxygenase, ADI1, ARD, ARD1, human aci-reductone dioxygenase 1, membrane-type 1 matrix metalloproteinase cytoplasmic tail binding protein-1, MtnD, Ni(II)-ARD

ECTree

     1 Oxidoreductases
         1.13 Acting on single donors with incorporation of molecular oxygen (oxygenases)
             1.13.11 With incorporation of two atoms of oxygen
                1.13.11.53 acireductone dioxygenase (Ni2+-requiring)

Crystallization

Crystallization on EC 1.13.11.53 - acireductone dioxygenase (Ni2+-requiring)

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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
crystal structure analysis
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quantum-classical dynamics simulations with Co2+ bound. Both Fe2+-like (reaction of EC 1.13.11.54) and Ni2+-like (reaction of EC 1.13.11.53) routes are accessible to Co2+-ARD. with low spin Co2+, the reaction exclusively follows the Fe2+-dependent pathways, producing alpha-keto acid precursor of methionine and formate, while the high spin Co2+ path contains a bifurcation in the pathway that follows along both the Fe2+-dependent pathway and Ni2+-dependent pathway that produces methylthiopropionate, carbon monoxide and formate
nanodroplet vapour diffusion method using 19.0% (w/v) polyethylene glycol 4000, 19.0% (w/v) isopropanol, 5.0% glycerol, and 0.095 M Na-citrate pH 4.2 (final pH 5.6)
Ni- and Co-bound proteins. Both Ni and Co present an octahedral coordination geometry in the active site bound to protein ligands H88, H90, H133 and E94. Additionally, two distinct water (or hydroxide) ligands bind to the metal ion center
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