Literature DB >> 23837

Methylamine dehydrogenase of Pseudomonase sp. J Isolation and properties of the subunits.

T Matsumoto, B Y Hiraoka, J Tobari.   

Abstract

Two kinds of subunits, light subunit (Mr =1300) and heavy subunit (Mr=40 000), were isolated from a methylamine dehydrogenase (Mr=105 000) of Pseudomonas sp. J. The isolation of the subunits was carried out by gel chromatography after the enzyme had been treated with 3M guanidine-HCl. Coexistence of both of the subunit exhibited an absorption maximum only at 278 nm but in addition to the peak at 278 nm. The results indicate that the prosthetic group, assumed to be a derivative of pyridoxal, was bound to the light subunit. The spectral changes of the light subunit were observed by addition of methylamine. Various physical and biochemical parameters of the subunits are reported.

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Year:  1978        PMID: 23837     DOI: 10.1016/0005-2744(78)90064-5

Source DB:  PubMed          Journal:  Biochim Biophys Acta        ISSN: 0006-3002


  8 in total

1.  Localization of periplasmic redox proteins of Alcaligenes faecalis by a modified general method for fractionating gram-negative bacteria.

Authors:  Z Zhu; D Sun; V L Davidson
Journal:  J Bacteriol       Date:  1999-10       Impact factor: 3.490

2.  Genetic organization of methylamine utilization genes from Methylobacterium extorquens AM1.

Authors:  A Y Chistoserdov; Y D Tsygankov; M E Lidstrom
Journal:  J Bacteriol       Date:  1991-09       Impact factor: 3.490

Review 3.  Quinoproteins in C1-dissimilation by bacteria.

Authors:  C Anthony
Journal:  Antonie Van Leeuwenhoek       Date:  1989-05       Impact factor: 2.271

4.  Two distinct azurins function in the electron-transport chain of the obligate methylotroph Methylomonas J.

Authors:  R P Ambler; J Tobari
Journal:  Biochem J       Date:  1989-07-15       Impact factor: 3.857

5.  Purification and properties of methylamine dehydrogenase from Paracoccus denitrificans.

Authors:  M Husain; V L Davidson
Journal:  J Bacteriol       Date:  1987-04       Impact factor: 3.490

Review 6.  Quinoprotein-catalysed reactions.

Authors:  C Anthony
Journal:  Biochem J       Date:  1996-12-15       Impact factor: 3.857

7.  Amine dehydrogenase of Pseudomonas putida: properties of the heme-prosthetic group.

Authors:  D R Durham; J J Perry
Journal:  J Bacteriol       Date:  1978-09       Impact factor: 3.490

8.  The role of blue copper proteins in the oxidation of methylamine by an obligate methylotroph.

Authors:  S A Lawton; C Anthony
Journal:  Biochem J       Date:  1985-06-15       Impact factor: 3.857

  8 in total

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