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Literature summary for 1.8.3.1 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)

Cloned (Comment) Organism
recombinant R160Q Homo sapiens

Protein Variants

Protein Variants Comment Organism
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

Metals/Ions Comment Organism Structure
Mo
-
Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant R160Q Homo sapiens

Substrates and Products (Substrate)

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