Home LiteratureArticle Details
PMID: 4323962 Published · ppublish English Journal Article

Comparative biochemical and immunological study of malic enzyme from two species of lactic acid bacteria: evolutionary implications.

Journal of bacteriology ·Vol. 106 ·No. 1 ·1971-04-00 ·Pages 126-37

London J, Meyer EY, Kulczyk S

Abstract

Representatives of both Streptococcus faecalis and Lactobacillus casei produce isofunctional malic enzymes. All 10 strains of S. faecalis tested could be induced to synthesize malic enzyme and readily adapted to growth on malate. Although 17 of 21 L. casei strains could be induced to produce malic enzyme, only 9 of 14 strains tested grew at the expense of malate. A comparison of catalytic and regulatory properties suggested that the malic enzymes from S. faecalis and L. casei were very similar. Immunological analyses showed that the numerous similarities in function actually reflected partial protein homologies; however, two distinct forms of the malic enzyme were detected among different strains of L. casei by immunochemical and serological procedures. The division of L. casei into two subgroups based on the immunological type of malic enzyme synthesized corresponds to two subspecies currently recognized by microbial taxonomists.

MeSH Terms
Acrylates Animals Biological Evolution Cell-Free System Chromatography, DEAE-Cellulose Complement Fixation Tests Culture Media Electrophoresis, Disc Enterococcus faecalis/classification,enzymology,growth & development,immunology,metabolism Gels Immune Sera Immunodiffusion Immunoelectrophoresis Lactobacillus/classification,enzymology,growth & development,immunology,metabolism Malate Dehydrogenase/isolation & purification,metabolism Malates/metabolism NAD/metabolism Precipitin Tests Rabbits Species Specificity Spectrophotometry
Chemicals
Acrylates Culture Media Gels Immune Sera Malates NAD Malate Dehydrogenase
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
London J
Meyer E Y
Kulczyk S
References (19)
19 references, click to expand
  1. Direct quantitative gas chromatographic separation of C2-C6 fatty acids, methanol, and ethyl alcohol in aqueous microbial fermentation media.
    Appl Microbiol. 1968 Feb;16(2):285-90 PMID: 5645415
  2. Immunological prediction of sequence differences among proteins. Chemical comparison of chicken, quail, and phesant lysozymes.
    J Biol Chem. 1969 Apr 25;244(8):2085-94 PMID: 4889463
  3. Non-Darwinian evolution.
    Science. 1969 May 16;164(3881):788-98 PMID: 5767777
  4. Malate utilization by a group D Streptococcus. II. Evidence for allosteric inhibition of an inducible malate dehydrogenase (decarboxylating) by ATP and glycolytic intermediate products.
    Biochim Biophys Acta. 1969 Apr 22;178(2):205-12 PMID: 4977226
  5. Malate utilization by a group D Streptococcus: physiological properties and purification of an inducible malic enzyme.
    J Bacteriol. 1969 May;98(2):705-11 PMID: 4306540
  6. Malate utilization by a group D Streptococcus: regulation of malic enzyme synthesis by an inducible malate permease.
    J Bacteriol. 1970 Apr;102(1):130-7 PMID: 5437724
  7. Comparative allostery of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthetase as a molecular basis for classification.
    J Bacteriol. 1970 Mar;101(3):763-9 PMID: 4985590
  8. Taxonomic implications of temperature dependence of the allosteric inhibition of 3-deoxy-D-arabino-heptulosonate 7-phosphate synthetase in Bacillus.
    J Bacteriol. 1970 May;102(2):489-97 PMID: 5419264
  9. Biosynthesis of dicarboxylic acids by carbon dioxide fixation. IV. Isolation and properties of an adaptive "malic" enzyme from Lactobacillus arabinosus.
    J Biol Chem. 1950 Dec;187(2):891-905 PMID: 14803472
  10. Protein measurement with the Folin phenol reagent.
    J Biol Chem. 1951 Nov;193(1):265-75 PMID: 14907713
  11. Species differentiation of oral lactobacilli from man including description of Lactobacillus salivarius nov spec and lactobacillus Cellobiosus nov spec.
    J Bacteriol. 1953 Jun;65(6):681-99 PMID: 13069442
  12. A comparative study of the structures of bovine and ovine pancreatic ribonucleases.
    J Biol Chem. 1959 May;234(5):1118-23 PMID: 13654331
  13. Quantitative micro-complement fixation and its use in the study of antigenic structure by specific antigen-antibody inhibition.
    J Immunol. 1961 Sep;87:290-5 PMID: 13783305
  14. Immunological studies with genetically altered beta-galactosidases.
    Ann N Y Acad Sci. 1963 May 8;103:1058-66 PMID: 13942583
  15. ANTICOMPLEMENTARY EFFECTS AND COMPLEMENT ACTIVITY OF HUMAN SERA.
    Proc Soc Exp Biol Med. 1964 Oct;117:292-7 PMID: 14229093
  16. EVOLUTION OF LACTIC DEHYDROGENASES.
    Fed Proc. 1964 Nov-Dec;23:1258-66 PMID: 14236134
  17. DISC ELECTROPHORESIS. II. METHOD AND APPLICATION TO HUMAN SERUM PROTEINS.
    Ann N Y Acad Sci. 1964 Dec 28;121:404-27 PMID: 14240539
  18. ANTIBODIES TO HUMAN A1 HEMOGLOBIN AND THEIR REACTION WITH A2, S, C, AND H HEMOGLOBINS.
    Immunochemistry. 1964 Apr;1:21-30 PMID: 14250012
  19. A correlation of antigenic characteristics among certain bacteria of the Lactobacillus group.
    J Infect Dis. 1950 Jan-Feb;86(1):63-80 PMID: 15402292
Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1971-04-00
Pages
126-37
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC248652
Subset
IM
Analysis Services
Analysis Services

Contact

No. 2 Wenbo Road, Zhangqiu District, Jinan, Shandong

Qilu Normal University · Genelibs Bioinformatics Lab

750 Shunhua Rd, Jinan

2F, Bldg F, University Science Park

Tel: 0531-88819269

WeChat Official Account

Follow our WeChat subscription account for real-time updates and the latest in medical and biological research.


Business Email

E-mail: [email protected]