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Literature summary extracted from

  • Astashkin, A.V.; Johnson-Winters, K.; Klein, E.L.; Feng, C.; Wilson, H.L.; Rajagopalan, K.V.; Raitsimring, A.M.; Enemark, J.H.
    Structural studies of the molybdenum center of the pathogenic R160Q mutant of human sulfite oxidase by pulsed EPR spectroscopy and 17O and 33S labeling (2008), J. Am. Chem. Soc., 130, 8471-8480.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.8.3.1 recombinant R160Q Homo sapiens

Protein Variants

EC Number Protein Variants Comment Organism
1.8.3.1 R160Q at least three different Mo(V) species of R160Q exist as a function of pH (low pH type 1 and type 2, and high-pH). Mo(V) species with a blocked form of sulfite oxidase, with sulfate coordinated to the Mo center is the only species at pH higher or equal as 6 and remains a significant form at physiological pH, is six-coordinate and has a nearby exchangeable proton that is likely to be hydrogen-bonded to an oxygen of the sulfate ligand. The blocked structure of R160Q represents a catalytic dead end that contributes to the lethality of this mutant under physiological conditions Homo sapiens

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.8.3.1 Mo
-
 Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.8.3.1 Homo sapiens
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.8.3.1 recombinant R160Q Homo sapiens

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.8.3.1 sulfite + H2O + A
-
 Homo sapiens sulfate + AH2
-
 ?