Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Homologues of the genes cysB, cysI, cysH, cysD, cysN, and selD were identified in the genome of the phototrophic purple sulfur bacterium Allochromatium vinosum (formerly Chromatium vinosum). On the basis of amino acid comparisons these genes encode a ferredoxin-dependent siroheme-sulfite reductase (CysI), a plant-type assimilatory APS reductase without thioredoxin domain (CysH), the two different subunits of heterodimeric ATP sulfurylase (CysDN), a transcriptional regulator (CysB) and a selenophosphate synthase (SelD). cysIHDN appear to form an operon and are preceded by cysB which is transcribed in the opposite direction. SelD is situated downstream of cysN and transcribed divergently to cysIHDN. The lack of a gene for APS kinase and presence of a gene for an assimilatory APS reductase implies that assimilatory sulfate reduction in A. vinosum proceeds along the pathway suggested for higher plants without intermediary formation of PAPS. Two completely separate pathways involving specialized enzymes are used for assimilatory sulfate reduction and dissimilatory sulfur oxidation in A. vinosum. The presence of cysB indicates that the genes for assimilatory sulfate reduction are expressed only in the absence of reduced sulfur compounds.
Mol Biol Rep 2000 Mar
PMID:Characterization of the cys gene locus from Allochromatium vinosum indicates an unusual sulfate assimilation pathway. 1093 23

Selenophosphate synthetase (EC 2.7.9.3), the product of the selD gene, produces the biologically active selenium donor compound, monoselenophosphate, from ATP and selenide, for the synthesis of selenocysteine. The kinetoplastid Leishmania major and Trypanosoma brucei selD genes were cloned and the SELD protein overexpressed and purified to apparent homogeneity. The selD gene in L. major and T. brucei are respectively 1197 and 1179 bp long encoding proteins of 399 and 393 amino acids with molecular masses of 42.7 and 43 kDa. The molecular mass of 100 kDa for both (L. major and T. brucei) SELDs is consistent with dimeric proteins. The kinetoplastid selD complement Escherichia coli (WL400) selD deletion confirming it is a functional enzyme and the specific activity of these enzymes was determined. A conserved Cys residue was identified both by multiple sequence alignment as well as by functional complementation and activity assay of the mutant (Cys to Ala) forms of the SELD identifying this residue as essential for the catalytic function.
Mol Biochem Parasitol 2008 Dec
PMID:Selenocysteine incorporation in Kinetoplastid: selenophosphate synthetase (SELD) from Leishmania major and Trypanosoma brucei. 1881 92