Literature DB >> 12501417

A Class II fructose-1,6-bisphosphate aldolase from a halophilic archaebacterium Haloferax mediterranei.

Sandra E. D'Souza1, Wijaya Altekar.   

Abstract

Fructose-1,6-bisphosphate (FBP) aldolase (EC 4.1.2.13) was purified 97-fold from a halophilic archaebacterium Haloferax mediterranei, with a specific activity of 2.8. The enzyme was characterized as a Class II aldolase on the basis of its inhibition by EDTA and other metal chelators. The enzyme had a specific requirement for divalent metal Fe(2+) for activity. Sulfhydryl compounds enhanced aldolase activity.

Entities:  

Year:  1998        PMID： 12501417     DOI： 10.2323/jgam.44.235

Source DB:  PubMed          Journal:  J Gen Appl Microbiol        ISSN： 0022-1260            Impact factor:   1.452


  3 in total

Review 1.  Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.

Authors:  Christopher Bräsen; Dominik Esser; Bernadette Rauch; Bettina Siebers
Journal:  Microbiol Mol Biol Rev       Date:  2014-03       Impact factor: 11.056

Review 2.  Distribution and phylogenies of enzymes of the Embden-Meyerhof-Parnas pathway from archaea and hyperthermophilic bacteria support a gluconeogenic origin of metabolism.

Authors:  Ron S Ronimus; Hugh W Morgan
Journal:  Archaea       Date:  2003-10       Impact factor: 3.273

3.  Fructose degradation in the haloarchaeon Haloferax volcanii involves a bacterial type phosphoenolpyruvate-dependent phosphotransferase system, fructose-1-phosphate kinase, and class II fructose-1,6-bisphosphate aldolase.

Authors:  Andreas Pickl; Ulrike Johnsen; Peter Schönheit
Journal:  J Bacteriol       Date:  2012-04-06       Impact factor: 3.490
  3 in total

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