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. 1988 Feb;170(2):751–756. doi: 10.1128/jb.170.2.751-756.1988

Purification and characterization of Clostridium sticklandii D-selenocystine alpha, beta-lyase.

N Esaki 1, V Seraneeprakarn 1, H Tanaka 1, K Soda 1
PMCID: PMC210718  PMID: 3338973

Abstract

We have found a novel enzyme that decomposes D-selenocystine into pyruvate, ammonia, and elemental selenium in extracts of Clostridium sticklandii and C. sporogenes. The enzyme of C. sticklandii has been purified to homogeneity. It has a molecular weight of 74,000 and consists of two subunits identical in molecular weight (35,000). Pyridoxal 5'-phosphate is required as a cofactor. In addition to D-selenocystine, D-cystine, D-lanthionine, meso-lanthionine, and D-cysteine serve as substrates. However, D-selenocysteine, D-serine, DL-selenohomocystine, and L-amino acids are inert. The enzyme also catalyzes the beta-replacement reaction between D-selenocystine and a thiol to produce S-substituted D-cysteine. L-Selenohomocysteine also can serve as a substituent donor in the beta-replacement reaction to yield selenocystathionine.

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Selected References

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