Tags

Type your tag names separated by a space and hit enter

Glucose-6-phosphate dehydrogenase from the chemolithotroph Thiobacillus ferrooxidans.
J Bacteriol. 1971 Oct; 108(1):343-52.JB

Abstract

Glucose-6-phosphate dehydrogenase was partially purified from both glucose-grown and iron-glucose-grown Thiobacillus ferrooxidans. The enzyme possesses a dual nucleotide specificity for either nicotinamide adenine dinucleotide phosphate (NADP) or nicotinamide adenine dinucleotide (NAD) and has a molecular weight of 110,000 as determined by gel electrophoresis. Evidence is presented that T. ferrooxidans glucose-6-phosphate dehydrogenase is identical when isolated from cells grown mixotrophically (iron-glucose grown) or cells grown heterotrophically (glucose-grown cells). The enzyme is activated by Mg(2+), and to a lesser extent by low concentrations of Mn(2+). Reduced NAD inhibits the enzyme from T. ferrooxidans. No deviation from normal Michaelis-Menten kinetics was observed in velocity versus substrate concentration experiments. Adenosine triphosphate exerted a profound inhibition of the enzyme; the effect was 10 times more pronounced in the presence of NAD as compared to NADP. The physiological significance of this inhibition is discussed.

Authors

No affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article

Language

eng

PubMed ID

4399340

Citation

Tabita, R, and D G. Lundgren. "Glucose-6-phosphate Dehydrogenase From the Chemolithotroph Thiobacillus Ferrooxidans." Journal of Bacteriology, vol. 108, no. 1, 1971, pp. 343-52.
Tabita R, Lundgren DG. Glucose-6-phosphate dehydrogenase from the chemolithotroph Thiobacillus ferrooxidans. J Bacteriol. 1971;108(1):343-52.
Tabita, R., & Lundgren, D. G. (1971). Glucose-6-phosphate dehydrogenase from the chemolithotroph Thiobacillus ferrooxidans. Journal of Bacteriology, 108(1), 343-52.
Tabita R, Lundgren DG. Glucose-6-phosphate Dehydrogenase From the Chemolithotroph Thiobacillus Ferrooxidans. J Bacteriol. 1971;108(1):343-52. PubMed PMID: 4399340.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Glucose-6-phosphate dehydrogenase from the chemolithotroph Thiobacillus ferrooxidans. AU - Tabita,R, AU - Lundgren,D G, PY - 1971/10/1/pubmed PY - 1971/10/1/medline PY - 1971/10/1/entrez SP - 343 EP - 52 JF - Journal of bacteriology JO - J. Bacteriol. VL - 108 IS - 1 N2 - Glucose-6-phosphate dehydrogenase was partially purified from both glucose-grown and iron-glucose-grown Thiobacillus ferrooxidans. The enzyme possesses a dual nucleotide specificity for either nicotinamide adenine dinucleotide phosphate (NADP) or nicotinamide adenine dinucleotide (NAD) and has a molecular weight of 110,000 as determined by gel electrophoresis. Evidence is presented that T. ferrooxidans glucose-6-phosphate dehydrogenase is identical when isolated from cells grown mixotrophically (iron-glucose grown) or cells grown heterotrophically (glucose-grown cells). The enzyme is activated by Mg(2+), and to a lesser extent by low concentrations of Mn(2+). Reduced NAD inhibits the enzyme from T. ferrooxidans. No deviation from normal Michaelis-Menten kinetics was observed in velocity versus substrate concentration experiments. Adenosine triphosphate exerted a profound inhibition of the enzyme; the effect was 10 times more pronounced in the presence of NAD as compared to NADP. The physiological significance of this inhibition is discussed. SN - 0021-9193 UR - https://www.unboundmedicine.com/medline/citation/4399340/Glucose_6_phosphate_dehydrogenase_from_the_chemolithotroph_Thiobacillus_ferrooxidans_ L2 - http://jb.asm.org/cgi/pmidlookup?view=long&pmid=4399340 DB - PRIME DP - Unbound Medicine ER -