Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.8.3.1 extracted from

  • Low, L.; Ryan Kilmartin, J.; Bernhardt, P.; Kappler, U.
    How are "atypical" sulfite dehydrogenases linked to cell metabolism? Interactions between the sort sulfite dehydrogenase and small redox proteins (2011), Front. Microbiol., 2, 58.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.8.3.1

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Sinorhizobium meliloti

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm
-
 Sinorhizobium meliloti 5737
-

Metals/Ions

Metals/Ions Comment Organism Structure
Molybdenum recombinant enzyme contains 0.69 molecules of Mo per protein subunit Sinorhizobium meliloti

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
42669
-
 2 * 42669, mass spectrometry, 2 * 42791, calculated Sinorhizobium meliloti
42791
-
 2 * 42669, mass spectrometry, 2 * 42791, calculated Sinorhizobium meliloti
71000
-
 gel filtration Sinorhizobium meliloti

Organism

Organism UniProt Comment Textmining
Sinorhizobium meliloti F7X8Y3
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
sulfite + cytochrome c substrates horse heart cytochrome c, and recombinant Starkeya novella cytochrome c are only reduced to about 40% while Sinorhizobium meliloti cytochrome c is almost completely reduced. Enzyme interacts with two small redox proteins, a cytochrome c and a Cu containing pseudoazurin, that are encoded in the same operon and are co-transcribed with the sorT gene Sinorhizobium meliloti sulfate + reduced cytochrome c
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 42669, mass spectrometry, 2 * 42791, calculated Sinorhizobium meliloti

Synonyms

Synonyms Comment Organism
SorT
-
 Sinorhizobium meliloti

General Information

General Information Comment Organism
physiological function enzyme is able to couple efficiently to a cytochrome c isolated from the same organism despite being unable to efficiently reduce horse heart cytochrome c. Enzyme interacts with two small redox proteins, a cytochrome c and a Cu containing pseudoazurin, that are encoded in the same operon and are co-transcribed with the sorT gene. The pseudoazurin may act as an intermediate electron shuttle between. The protein system appears to couple directly to the respiratory chain, most likely to a cytochrome oxidase Sinorhizobium meliloti