دورية أكاديمية
أعرض في EDS

Pyruvate kinase 2 from Synechocystis sp. PCC 6803 increased substrate affinity via glucose-6-phosphate and ribose-5-phosphate for phosphoenolpyruvate consumption.

التفاصيل البيبلوغرافية
العنوان: Pyruvate kinase 2 from Synechocystis sp. PCC 6803 increased substrate affinity via glucose-6-phosphate and ribose-5-phosphate for phosphoenolpyruvate consumption.
المؤلفون: Karikomi M; School of Agriculture, Meiji University, 1-1-1, Higashimita, Tama-Ku, Kawasaki, Kanagawa, 214-8571, Japan., Katayama N; School of Agriculture, Meiji University, 1-1-1, Higashimita, Tama-Ku, Kawasaki, Kanagawa, 214-8571, Japan., Osanai T; School of Agriculture, Meiji University, 1-1-1, Higashimita, Tama-Ku, Kawasaki, Kanagawa, 214-8571, Japan. tosanai@meiji.ac.jp.
المصدر: Plant molecular biology [Plant Mol Biol] 2024 May 17; Vol. 114 (3), pp. 60. Date of Electronic Publication: 2024 May 17.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: Kluwer Academic Country of Publication: Netherlands NLM ID: 9106343 Publication Model: Electronic Cited Medium: Internet ISSN: 1573-5028 (Electronic) Linking ISSN: 01674412 NLM ISO Abbreviation: Plant Mol Biol Subsets: MEDLINE
أسماء مطبوعة: Publication: Dordrecht : Kluwer Academic
Original Publication: The Hague ; Boston : Martinus Nijhoff/Dr. W. Junk, 1981-
مواضيع طبية MeSH: Synechocystis*/metabolism , Synechocystis*/genetics , Pyruvate Kinase*/metabolism , Pyruvate Kinase*/genetics , Phosphoenolpyruvate*/metabolism , Glucose-6-Phosphate*/metabolism , Ribosemonophosphates*/metabolism, Substrate Specificity ; Hydrogen-Ion Concentration ; Bacterial Proteins/metabolism ; Bacterial Proteins/genetics ; Kinetics ; Temperature
مستخلص: Pyruvate kinase (Pyk, EC 2.7.1.40) is a glycolytic enzyme that generates pyruvate and adenosine triphosphate (ATP) from phosphoenolpyruvate (PEP) and adenosine diphosphate (ADP), respectively. Pyk couples pyruvate and tricarboxylic acid metabolisms. Synechocystis sp. PCC 6803 possesses two pyk genes (encoded pyk1, sll0587 and pyk2, sll1275). A previous study suggested that pyk2 and not pyk1 is essential for cell viability; however, its biochemical analysis is yet to be performed. Herein, we biochemically analyzed Synechocystis Pyk2 (hereafter, SyPyk2). The optimum pH and temperature of SyPyk2 were 7.0 and 55 °C, respectively, and the K m values for PEP and ADP under optimal conditions were 1.5 and 0.053 mM, respectively. SyPyk2 is activated in the presence of glucose-6-phosphate (G6P) and ribose-5-phosphate (R5P); however, it remains unaltered in the presence of adenosine monophosphate (AMP) or fructose-1,6-bisphosphate. These results indicate that SyPyk2 is classified as PykA type rather than PykF, stimulated by sugar monophosphates, such as G6P and R5P, but not by AMP. SyPyk2, considering substrate affinity and effectors, can play pivotal roles in sugar catabolism under nonphotosynthetic conditions.
(© 2024. The Author(s).)
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معلومات مُعتمدة: JPMJAL1306 Japan Science and Technology Corporation; 20H02905 Japan Society for the Promotion of Science
فهرسة مساهمة: Keywords: Synechocystis sp. PCC 6803; Glycolysis; Microalgae; Pyruvate kinase
المشرفين على المادة: 0 (ribose-5-phosphate)
تواريخ الأحداث: Date Created: 20240517 Date Completed: 20240517 Latest Revision: 20240626
رمز التحديث: 20240626
مُعرف محوري في PubMed: PMC11101554
DOI: 10.1007/s11103-023-01401-0
PMID: 38758412
قاعدة البيانات: MEDLINE
الوصف
تدمد:1573-5028
DOI:10.1007/s11103-023-01401-0