Literature DB >> 1991505

Identification of sulfurtransferase enzymes in Azotobacter vinelandii.

S Pagani1, E Franchi, R Colnaghi, C Kennedy.   

Abstract

Rhodanese and 3-mercaptopyruvate sulphurtransferase have been identified in A. vinelandii. Two distinct active fractions of the two sulphur transferases were obtained after FPLC ion-exchange chromatography of material partially purified from crude extracts. Rhodanese has been purified to homogeneity, and it consists of one polypeptide chain of Mr ca 25,000. A partial purification of 3-mercaptopyruvate sulphurtransferase was obtained.

Entities:  

Mesh：

Substances：

Year:  1991        PMID： 1991505     DOI： 10.1016/0014-5793(91)80105-c

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  3 in total

1.  Backbone NMR assignment of the 29.6 kDa rhodanese protein from Azotobacter vinelandii.

Authors:  Mariana Gallo; Sonia Melino; Riccardo Melis; Maurizio Paci; Daniel O Cicero
Journal:  J Biomol NMR       Date:  2006-08-24       Impact factor: 2.835

Review 2.  Microbes and microbial enzymes for cyanide degradation.

Authors:  S A Raybuck
Journal:  Biodegradation       Date:  1992       Impact factor: 3.909

3.  Metatranscriptomic analysis of a high-sulfide aquatic spring reveals insights into sulfur cycling and unexpected aerobic metabolism.

Authors:  Anne M Spain; Mostafa S Elshahed; Fares Z Najar; Lee R Krumholz
Journal:  PeerJ       Date:  2015-09-22       Impact factor: 2.984
  3 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.