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Literature DB >> 643076

The covalent and tertiary structure of bovine liver rhodanese.

J H Ploegman, G Drent, K H Kalk, W G Hol, R L Heinrikson, P Keim, L Weng, J Russell.

Abstract

Bovine liver rhodanese is a single polypeptide of 293 amino acids in which the halves of the molecule assume analogous tertiary structures in the absence of substantial sequence homology. The sulphur atom transferred during catalysis is bound in persulphide linkage to Cys-247. Substrate binding seems to involve Arg-186 and Lys-249.

Entities: Chemical Gene Species

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Year: 1978 PMID： 643076 DOI： 10.1038/273124a0

Source DB: PubMed Journal: Nature ISSN： 0028-0836 Impact factor: 49.962

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Cited

38 in total

1. Active-site sulfhydryl chemistry plays a major role in the misfolding of urea-denatured rhodanese.

Authors: M Panda; P M Horowitz
Journal: J Protein Chem Date: 2000-07

2. The structure of apo protein-tyrosine phosphatase 1B C215S mutant: more than just an S --> O change.

Authors: G Scapin; S Patel; V Patel; B Kennedy; E Asante-Appiah
Journal: Protein Sci Date: 2001-08 Impact factor: 6.725

Review 3. The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations.

Authors: Domenico Bordo; Peer Bork
Journal: EMBO Rep Date: 2002-08 Impact factor: 8.807

4. Active rhodanese lacking nonessential sulfhydryl groups has increased hydrophobic exposure not observed in wild-type enzyme.

Authors: Yogeet Kaur; Jesse Ybarra; Paul M Horowitz
Journal: Protein J Date: 2004-05 Impact factor: 2.371

10. Immunological evidence for a conformational difference between recombinant bovine rhodanese and rhodanese purified from bovine liver.

Authors: G A Merrill; D Miller; J Chirgwin; P M Horowitz
Journal: J Protein Chem Date: 1992-04

The covalent and tertiary structure of bovine liver rhodanese.

1. Active-site sulfhydryl chemistry plays a major role in the misfolding of urea-denatured rhodanese.

2. The structure of apo protein-tyrosine phosphatase 1B C215S mutant: more than just an S --> O change.

Review 3. The rhodanese/Cdc25 phosphatase superfamily. Sequence-structure-function relations.

4. Active rhodanese lacking nonessential sulfhydryl groups has increased hydrophobic exposure not observed in wild-type enzyme.

5. Primary structure of avian hepatic rhodanese.

6. Synthesis of rhodanese in Hep 3B cells.

7. Crystal structure of the MAP kinase binding domain and the catalytic domain of human MKP5.

8. Detection and analysis of protein aggregation with confocal single molecule fluorescence spectroscopy.

9. Studies of functionally important structural flexibility of thiosulfate sulfurtransferase.

10. Immunological evidence for a conformational difference between recombinant bovine rhodanese and rhodanese purified from bovine liver.