Literature DB >> 19431407

Studies of functionally important structural flexibility of thiosulfate sulfurtransferase.

P Horowitz.   

Abstract

Entities:  

Year:  1980        PMID： 19431407      PMCID： PMC1327372          DOI： 10.1016/S0006-3495(80)85005-3

Source DB:  PubMed          Journal:  Biophys J        ISSN： 0006-3495            Impact factor:   4.033


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  5 in total

1.  Studies of the N-bromosuccinimide inactivation of the enzyme rhodanese.

Authors:  K Guido; P Horowitz
Journal:  Biochim Biophys Acta       Date:  1977-11-23

2.  The interdependence of substrate and protein transformations in rhodanese catalysis. I. Enzyme interactions with substrate, product, and inhibitor anions.

Authors:  S F Wang; M Volini
Journal:  J Biol Chem       Date:  1973-11-10       Impact factor: 5.157

3.  The interdependence of substrate and protein transformations in rhodanese catalysis. II. Enzyme conformational changes significant for catalysis.

Authors:  M Volini; S F Wang
Journal:  J Biol Chem       Date:  1973-11-10       Impact factor: 5.157

4.  The covalent and tertiary structure of bovine liver rhodanese.

Authors:  J H Ploegman; G Drent; K H Kalk; W G Hol; R L Heinrikson; P Keim; L Weng; J Russell
Journal:  Nature       Date:  1978-05-11       Impact factor: 49.962

5.  Active site cysteinyl and arginyl residues of rhodanese. A novel formation of disulfide bonds in the active site promoted by phenylglyoxal.

Authors:  L Weng; R L Heinrikson; J Westley
Journal:  J Biol Chem       Date:  1978-11-25       Impact factor: 5.157
  5 in total

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