Tags

Type your tag names separated by a space and hit enter

Inhibition by fructose 1,6-bisphosphate of transaldolase from Escherichia coli.
FEMS Microbiol Lett. 2016 09; 363(17)FM

Abstract

The effect of fructose 1,6-bisphosphate (Fru 1,6-P2) on the regulatory enzymes of pentose phosphate pathway of Escherichia coli was examined. Fru 1,6-P2 inhibited E. coli transaldolase (EC 2.2.1.2) competitively against fructose 6-phosphate and uncompetitively against erythrose 4-phosphate, whereas Fru 1,6-P2 did not affect glucose 6-phosphate dehydrogenase (EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (EC 1.1.1.44). Kinetic results can be explained by assuming that transaldolase has two kinds of binding sites for Fru 1,6-P2: a competitive binding site for fructose 6-phosphate and a second binding site on the enzyme-erythrose 4-phosphate complex. Fru 1,6-P2 increased resulting from the stimulation of glycolysis, can inhibit transaldolase and further participates in the elevation of the concentration of ribose 5-phosphate that can be preferentially utilized for anabolic reaction in exponential phase of E. coli.

Authors+Show Affiliations

Department of Biochemistry, School of Medicine, Aichi Medical University, Yazako-Karimata 1-1, Nagakute, Aichi 480-1195, Japan.Department of Biochemistry, School of Medicine, Aichi Medical University, Yazako-Karimata 1-1, Nagakute, Aichi 480-1195, Japan.Department of Biochemistry, School of Medicine, Aichi Medical University, Yazako-Karimata 1-1, Nagakute, Aichi 480-1195, Japan yoshino@aichi-med-u.ac.jp.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

27481705

Citation

Ogawa, Tadashi, et al. "Inhibition By Fructose 1,6-bisphosphate of Transaldolase From Escherichia Coli." FEMS Microbiology Letters, vol. 363, no. 17, 2016.
Ogawa T, Murakami K, Yoshino M. Inhibition by fructose 1,6-bisphosphate of transaldolase from Escherichia coli. FEMS Microbiol Lett. 2016;363(17).
Ogawa, T., Murakami, K., & Yoshino, M. (2016). Inhibition by fructose 1,6-bisphosphate of transaldolase from Escherichia coli. FEMS Microbiology Letters, 363(17). https://doi.org/10.1093/femsle/fnw183
Ogawa T, Murakami K, Yoshino M. Inhibition By Fructose 1,6-bisphosphate of Transaldolase From Escherichia Coli. FEMS Microbiol Lett. 2016;363(17) PubMed PMID: 27481705.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Inhibition by fructose 1,6-bisphosphate of transaldolase from Escherichia coli. AU - Ogawa,Tadashi, AU - Murakami,Keiko, AU - Yoshino,Masataka, Y1 - 2016/07/31/ PY - 2016/07/26/accepted PY - 2016/8/3/entrez PY - 2016/8/3/pubmed PY - 2017/11/14/medline KW - E. coli KW - Fru 1,6-P2 KW - fructose 1,6-bisphosphate KW - inhibition KW - pentose phosphate pathway KW - transaldolase JF - FEMS microbiology letters JO - FEMS Microbiol. Lett. VL - 363 IS - 17 N2 - The effect of fructose 1,6-bisphosphate (Fru 1,6-P2) on the regulatory enzymes of pentose phosphate pathway of Escherichia coli was examined. Fru 1,6-P2 inhibited E. coli transaldolase (EC 2.2.1.2) competitively against fructose 6-phosphate and uncompetitively against erythrose 4-phosphate, whereas Fru 1,6-P2 did not affect glucose 6-phosphate dehydrogenase (EC 1.1.1.49) and 6-phosphogluconate dehydrogenase (EC 1.1.1.44). Kinetic results can be explained by assuming that transaldolase has two kinds of binding sites for Fru 1,6-P2: a competitive binding site for fructose 6-phosphate and a second binding site on the enzyme-erythrose 4-phosphate complex. Fru 1,6-P2 increased resulting from the stimulation of glycolysis, can inhibit transaldolase and further participates in the elevation of the concentration of ribose 5-phosphate that can be preferentially utilized for anabolic reaction in exponential phase of E. coli. SN - 1574-6968 UR - https://www.unboundmedicine.com/medline/citation/27481705/Inhibition_by_fructose_16_bisphosphate_of_transaldolase_from_Escherichia_coli_ L2 - https://academic.oup.com/femsle/article-lookup/doi/10.1093/femsle/fnw183 DB - PRIME DP - Unbound Medicine ER -