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Uva-DARE (Digital Academic Repository) UvA-DARE (Digital Academic Repository) Lactate dehydrogenase in the cyanobacterium Microcystis PCC7806 Moezelaar, H.R.; Teixeira De Mattos, M.J.; Stal, L.J. Publication date 1995 Published in FEMS Microbiology Letters Link to publication Citation for published version (APA): Moezelaar, H. R., Teixeira De Mattos, M. J., & Stal, L. J. (1995). Lactate dehydrogenase in the cyanobacterium Microcystis PCC7806. FEMS Microbiology Letters, 127, 47-50. General rights It is not permitted to download or to forward/distribute the text or part of it without the consent of the author(s) and/or copyright holder(s), other than for strictly personal, individual use, unless the work is under an open content license (like Creative Commons). Disclaimer/Complaints regulations If you believe that digital publication of certain material infringes any of your rights or (privacy) interests, please let the Library know, stating your reasons. In case of a legitimate complaint, the Library will make the material inaccessible and/or remove it from the website. Please Ask the Library: https://uba.uva.nl/en/contact, or a letter to: Library of the University of Amsterdam, Secretariat, Singel 425, 1012 WP Amsterdam, The Netherlands. You will be contacted as soon as possible. UvA-DARE is a service provided by the library of the University of Amsterdam (https://dare.uva.nl) Download date:26 Sep 2021 FJXMSMicrobiology Letters 127 (1995) 47-50 Lactate dehydrogenase in the cyanobacterium Microcystis PCC7806 Roy Moezelaar, M. Joost Teixeira de Mattos, Lucas J. Stal * Department of Microbiology, University ofAmsterdam, Nieuwe Achtergracht 127, 1018 WS Amsterdam, the Netherlands Received 14 December 1994; revised 22 January 1995; accepted 22 January 1995 Abstract The cyanobacterium Microcystis PCC7806 was found to possess an NAD-dependent lactate dehydrogenase (EC 1.1.1.27) which catalyzes the reduction of pyruvate to L-lactate. The enzyme required fructose 1,6-bisphosphate for activity and displayed positive cooperativity towards pyruvate. Lactate was not formed during fermentation by cell suspensions, possibly due to low intracellular concentrations of fructose 1,6-bisphosphate and/or pyruvate. Keywords: Cyanobacteria; Microcystis PCC7806; Fermentation; Lactate dehydrogenase; Fructose 1,6_bisphosphate; Enzyme regulation 1. Introduction been found: homolactic fermentation in Oscillatoria Zimnetica [3], heterolactic and homoacetic fermenta- In many cyanobacteria, glycogen is stored during tion in Oscillatoria limosa [4], homoacetic fermenta- photoautotrophic growth and used as energy source tion in Nostoc sp. strain Cc [5], and mixed acid in the dark [l]. Aerobically, glycogen is degraded via fermentation in Cyanothece PCC7822 [6]. Excretion the oxidative pentose phosphate pathway and of lactate under dark anoxic conditions has also been metabolic energy is generated by respiration. Part of reported for Synechococcus PCC6716 [7] and OsciZ- the glycogen may be used for biosynthetic purposes, latoria terebriformis [8]. Despite the diversity of as was shown for Oscillatoria agardhii [2]. In addi- fermentation patterns, lactate seems to be a common tion to aerobic respiration, some cyanobacteria are fermentation product among cyanobacteria. capable of fermentative energy generation. Such We have previously shown that the unicellular species have invariably been isolated from habitats cyanobacterium Microcystis PCC7806 was capable that become periodically anoxic. Remarkably, these of fermentation, using glycogen as substrate [9]. cyanobacteria are not restricted to a single fermenta- Glucose derived from glycogen was degraded via the tion pathway, but various fermentation types have Embden-Meyerhof-Pamas pathway and fermented to ethanol, acetate, CO, and H,. Although lactate was not among the fermentation products, we noted the presence of considerable activity of lactate dehydro- ?? Corresponding author. Tel: +31 (20) 5257090, Fax: +31 (20) 5257085; e-mail [email protected]. genase (LDH) in cell-free extracts. This suggests that 037%1097/95/$09.50 8 1995 Federation of European Microbiological Societies. All rights reserved SSDI 0378-1097(95)00036-4 48 R. Moezelaar et al. / FEMS Microbiology Letters 127 (1995) 47-50 during fermentation the activity of LDH in vivo is effectively regulated. In this paper we demonstrate that LDH from Microcystis PCC7806 requires the -- glycolytic intermediate fructose 1,6-bisphosphate for activity, and displays positive cooperativity towards its substrate pyruvate. 2. Materials and methods Cultivation of Microcystis PCC7806 and prepara- tion of cell-free extracts were described earlier [9]. 0 25 50 75 100 125 Lactate dehydrogenase (LDH; EC 1.1.1.27/28) was assayed spectrophotometrically as pyruvate-depen- Protein (pg) dent disappearance of NADH which was followed at Fig. 1. Lactate dehydrogenase activity in crude (open square) and 340 nm (e340 = 6.22 mM_’ cm-‘). A single beam desalted (filled square) cell-free extracts of Microcystis PCC7806. spectrophotometer was used which was equipped The reaction mixture contained 50 mM Hepes/KOH (pH 7.5), 5 with a thermostated cuvet holder kept at 25°C. In all mM MgCl,, 0.15 mM NADH, 5 mM pyruvate, and cell-free extract. The effect of fructose 1,6-bisphosphate on lactate dehy- cases the observed reaction rate was constant for at drogenase activity in crude (open circle) and desalted (filled least 2 min and, unless stated otherwise, linearly circle) cell-free extracts was tested at a concentration of 10 mM. proportional to the amount of cell-free extract added. One unit (U) of enzyme activity is defined as the amount of enzyme catalyzing the conversion of 1 we initially used a reaction mixture that contained pmol substrate or the formation of 1 pmol product buffer (pH 7.51, magnesium ions, NADH, and pyru- in 1 min. Specific activities are expressed as U (mg vate. However, the activities thus found were not protein)- *. Protein was determined according to linearly proportional to the amount of extract added Bradford [lo], using bovine serum albumin as a to the reaction mixture (Fig. 1). Increasing the amount standard. of extract resulted in higher activities than expected, Routinely, LDH activity was assayed in a reaction which suggests the presence of an activating com- mixture containing 50 mM Hepes/KOH (pH 7.5), 5 pound in the cell-free extract. In order to remove this mM MgCl,, 0.15 mM NADH, 10 mM fructose activator the cell-free extract was desalted through 1,6-bisphosphate (FBP), and cell-free extract. The Sephadex G25. In the desalted extract no LDH activ- reaction was started by the addition of pyruvate (5 ity could be detected, indicating an absolute require- mM). The effect of the concentration of FBP (O-10 ment of the enzyme for the activator. NAD-depen- mM) and pyruvate (O-10 mM) on enzyme activity dent LDHs in most streptococci and in some lacto- was examined using cell-free extracts that had been bacilli require fructose 16-bisphosphate (FBP) as an desalted over a Sephadex G25 column. activator for activity [ll]. It was found that FBP also To assess which enantiomer of lactate was formed, restored LDH activity in desalted extracts of Micro- reaction mixtures were boiled for 5 min to inactivate cystis PCC7806. In the presence of FBP activities of LDH. D- and L-lactate were determined enzymati- LDH were linearly proportional to the amounts of tally using Test-Combinations from Boehringer extract (Fig. 1). Also in crude cell-free extracts the (Mannheim, Germany). disproportionality of LDH activity and the amount of extract was abolishedelevated by the addition of FBP, but the activity was slightly lower than in 3. Results desalted cell-free extracts. The specific LDH activity in crude cell-free extracts, which was routinely deter- In order to assay lactate dehydrogenase (LDH) mined at 10 mM FBP, was 0.14-0.16 U (mg pro- activity in cell-free extracts of Microcystis PCC7806 tein)-‘. LDH activity was not detected when NADP R. Moezelaar et al. / FEMS Microbiology Letters 127 (1995) 47-50 49 (2.3) it was concluded that binding of pyruvate was positively cooperative. A slight inhibition was ob- served with pyruvate concentrations exceeding 5 mM. The effect of nucleotides and phosphate on LDH activity was tested at 2.5 mM. ATP and ADP inhib- ited the enzyme by 40 and 20% respectively, whereas no effect was observed with AMP and inorganic phosphate. 4. Discussion 0- 0 2 4 6 8 10 The data presented confirm that the cyanobac- Fructoee-1,Wirphosphate (mM) terium Microcysris PCC7806 possesses an NAD-de- Fig. 2. Effect of fructose 1,6-bisphosphate concentration on lactate pendent lactate dehydrogenase (LDH; EC 1.1 J-27) dehydrogenase activity in desalted cell-free extracta of Microcy- which reduces pyruvate to L-lactate. This enzyme, as tis PCC7806. The assay contained 5 mM pyruvate. The insert well as the o-lactate forming enzyme (EC 1.1.1.28), shows a Eadie-Hofstee plot of the data. has also been demonstrated in other cyanobacteria [4,7,12], or its presence has been implied due to excretion of L-lactate under dark anoxic conditions was used as cofactor. L-lactate was the product of [3,6,8]. However, the enzyme in Microcystis pyruvate reduction. PCC7806 is the first cyanobacterial LDH reported to Saturation of the enzyme with FBP followed require fructose 1,6-bisphosphate @BP) for activity. Michaelis-Menten kinetics (Fig. 2). An apparent K, This characteristic has been known for NAD-depen- value of 0.96 mM FBP was calculated from the dent LDHs in most streptococci and in some lacto- Eadie-Hofstee plot. LDH from Microcysris PCC7806 bacilli Ill]. displayed a sigmoidal relationship between activity The specific activity of LDH in Microcystis and pyruvate concentration (Fig. 31, indicating al- PCC7806 (0.14-0.16 U (mg protein)-’ at saturating losteric regulation. From the positive Hill coefficient FBP concentrations) is the highest reported for cyanobacterial cell-free extracts thus far, yet no lac- tate is formed during fermentation by cell suspen- sions 191. Instead, the pyruvate generated by the Embden-Meyerhof-Pamas pathway is further de- graded to ethanol, acetate, CO, and H,.
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