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Glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Lactobacillus casei: responses with different modulators.
Indian J Biochem Biophys. 1989 Oct; 26(5):329-33.IJ

Abstract

Glucose 6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) were separated and partially purified from glucose-grown cells of Lactobacillus casei. The enzymes had similar pH optima, thermosensitivity and molecular weights. They had different net charges and their pI values were 5.38 and 4.52, respectively. Histidine, arginine, lysine and cysteine residues were essential for the activity of G6PD, and all the above amino acids with the exception of lysine were required for 6PGD activity. Mg2+ activated 6PGD up to 15 mM concentration, above which it was inhibitory. It had no effect on G6PD activity. G6PD was specific for NADP+, but 6PGD showed some activity with NAD+ as the cofactor, although it was essentially NADP(+)-preferring. Both the enzymes, were inhibited by NADPH. 6PGD was also inhibited by its product, ribulose 5-phosphate. ATP inhibited 6PGD only at subsaturating concentrations of NADP+. The inhibition was sigmoidal in the absence of Mg2+ and hyperbolic in its presence.

Authors

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Pub Type(s)

Journal Article

Language

eng

PubMed ID

2516835

Citation

Menezes, L, et al. "Glucose 6-phosphate Dehydrogenase and 6-phosphogluconate Dehydrogenase From Lactobacillus Casei: Responses With Different Modulators." Indian Journal of Biochemistry & Biophysics, vol. 26, no. 5, 1989, pp. 329-33.
Menezes L, Kelkar SM, Kaklij GS. Glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Lactobacillus casei: responses with different modulators. Indian J Biochem Biophys. 1989;26(5):329-33.
Menezes, L., Kelkar, S. M., & Kaklij, G. S. (1989). Glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Lactobacillus casei: responses with different modulators. Indian Journal of Biochemistry & Biophysics, 26(5), 329-33.
Menezes L, Kelkar SM, Kaklij GS. Glucose 6-phosphate Dehydrogenase and 6-phosphogluconate Dehydrogenase From Lactobacillus Casei: Responses With Different Modulators. Indian J Biochem Biophys. 1989;26(5):329-33. PubMed PMID: 2516835.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Glucose 6-phosphate dehydrogenase and 6-phosphogluconate dehydrogenase from Lactobacillus casei: responses with different modulators. AU - Menezes,L, AU - Kelkar,S M, AU - Kaklij,G S, PY - 1989/10/1/pubmed PY - 1989/10/1/medline PY - 1989/10/1/entrez SP - 329 EP - 33 JF - Indian journal of biochemistry & biophysics JO - Indian J Biochem Biophys VL - 26 IS - 5 N2 - Glucose 6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) were separated and partially purified from glucose-grown cells of Lactobacillus casei. The enzymes had similar pH optima, thermosensitivity and molecular weights. They had different net charges and their pI values were 5.38 and 4.52, respectively. Histidine, arginine, lysine and cysteine residues were essential for the activity of G6PD, and all the above amino acids with the exception of lysine were required for 6PGD activity. Mg2+ activated 6PGD up to 15 mM concentration, above which it was inhibitory. It had no effect on G6PD activity. G6PD was specific for NADP+, but 6PGD showed some activity with NAD+ as the cofactor, although it was essentially NADP(+)-preferring. Both the enzymes, were inhibited by NADPH. 6PGD was also inhibited by its product, ribulose 5-phosphate. ATP inhibited 6PGD only at subsaturating concentrations of NADP+. The inhibition was sigmoidal in the absence of Mg2+ and hyperbolic in its presence. SN - 0301-1208 UR - https://www.unboundmedicine.com/medline/citation/2516835/Glucose_6_phosphate_dehydrogenase_and_6_phosphogluconate_dehydrogenase_from_Lactobacillus_casei:_responses_with_different_modulators_ L2 - https://antibodies.cancer.gov/detail/CPTC-GSTP1-1 DB - PRIME DP - Unbound Medicine ER -