Oligomeric Enzymes in the C4 Pathway of Photosynthesis

Overview

Journal Photosynth Res

Publisher Springer

Date 2014 Jan 15

PMID 24420581

Citations 2

Authors

F E Podesta

A A Iglesias

C S Andreo

Affiliations

Soon will be listed here.

Abstract

This review deals with the factors controlling the aggregation-state of several enzymes involved in C4 photosynthesis, namely phosphoenolpyruvate carboxylase, NAD-and NADP-malic enzyme, NADP-malic dehydrogenase and pyruvate, phosphate dikinase and its regulatory protein. All of these enzymes are oligomeric and have been shown to undergo changes in their quaternary structure in vitro under different conditions. The activity changes linked to variations in aggregation-state are discussed in terms of their putative physiological role in the regulation of C4 metabolism.

Citing Articles

Hysteretic properties of NADP-malic enzyme from sugarcane leaves.

Iglesias A, Andreo C Photosynth Res. 2014; 31(2):89-97.

PMID: 24407981 DOI: 10.1007/BF00028786.

Homologous genes for the C4 isoform of phosphoenolpyruvate carboxylase in a C3 and a C4 Flaveria species.

Hermans J, Westhoff P Mol Gen Genet. 1992; 234(2):275-84.

PMID: 1508152 DOI: 10.1007/BF00283848.

References

Baer G, Schrader L . Stabilization of pyruvate, pi dikinase regulatory protein in maize leaf extracts. Plant Physiol. 1985; 77(3):608-11. PMC: 1064572. DOI: 10.1104/pp.77.3.608. View

Budde R, Ernst S, Chollet R . Substrate specificity and regulation of the maize (Zea mays) leaf ADP: protein phosphotransferase catalysing phosphorylation/inactivation of pyruvate, orthophosphate dikinase. Biochem J. 1986; 236(2):579-84. PMC: 1146878. DOI: 10.1042/bj2360579. View

MCNAUGHTON G, Fewson C, Wilkins M, Nimmo H . Purification, oligomerization state and malate sensitivity of maize leaf phosphoenolpyruvate carboxylase. Biochem J. 1989; 261(2):349-55. PMC: 1138832. DOI: 10.1042/bj2610349. View

Hatch M, Slack C . The participation of phosphoenolpyruvate synthetase in photosynthetic CO2 fixation of tropical grasses. Arch Biochem Biophys. 1967; 120(1):224-5. DOI: 10.1016/0003-9861(67)90618-2. View

Frieden C . The regulation of protein polymerization. Trends Biochem Sci. 1989; 14(7):283-6. DOI: 10.1016/0968-0004(89)90065-0. View

Hausler R, Holtum J, Latzko E . CO2 is the inorganic carbon substrate of NADP malic enzymes from Zea mays and from wheat germ. Eur J Biochem. 1987; 163(3):619-26. DOI: 10.1111/j.1432-1033.1987.tb10911.x. View

Shirahashi K, Hayakawa S, Sugiyama T . Cold lability of pyruvate, orthophosphate dikinase in the maize leaf. Plant Physiol. 1978; 62(5):826-30. PMC: 1092230. DOI: 10.1104/pp.62.5.826. View

Ashton A, Hatch M . Regulation of C4 photosynthesis: physical and kinetic properties of active (dithiol) and inactive (disulfide) NADP-malate dehydrogenase from Zea mays. Arch Biochem Biophys. 1983; 227(2):406-15. DOI: 10.1016/0003-9861(83)90470-8. View

Krall J, Edwards G, Andreo C . Protection of Pyruvate,Pi Dikinase from Maize against Cold Lability by Compatible Solutes. Plant Physiol. 1989; 89(1):280-5. PMC: 1055832. DOI: 10.1104/pp.89.1.280. View

10.

Roeske C, Chollet R . Role of Metabolites in the Reversible Light Activation of Pyruvate, Orthophosphate Dikinase in Zea mays Mesophyll Cells in Vivo. Plant Physiol. 1989; 90(1):330-7. PMC: 1061718. DOI: 10.1104/pp.90.1.330. View

11.

Wagner R, Gonzalez D, Podesta F, Andreo C . Changes in the quaternary structure of phosphoenolpyruvate carboxylase induced by ionic strength affect its catalytic activity. Eur J Biochem. 1987; 164(3):661-6. DOI: 10.1111/j.1432-1033.1987.tb11177.x. View

12.

Podesta F, Andreo C . Maize leaf phosphoenolpyruvate carboxylase : oligomeric state and activity in the presence of glycerol. Plant Physiol. 1989; 90(2):427-33. PMC: 1061741. DOI: 10.1104/pp.90.2.427. View

13.

Gekko K, Timasheff S . Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry. 1981; 20(16):4667-76. DOI: 10.1021/bi00519a023. View

14.

Willeford K, Wedding R . pH Effects on the Activity and Regulation of the NAD Malic Enzyme. Plant Physiol. 1987; 84(4):1084-7. PMC: 1056732. DOI: 10.1104/pp.84.4.1084. View

15.

Gerlsma S . Reversible denaturation of ribonuclease in aqueous solutions as influenced by polyhydric alcohols and some other additives. J Biol Chem. 1968; 243(5):957-61. View

16.

Grover S, Wedding R . Kinetic Ramifications of the Association-Dissociation Behavior of NAD Malic Enzyme : A Possible Regulatory Mechanism. Plant Physiol. 1982; 70(4):1169-72. PMC: 1065845. DOI: 10.1104/pp.70.4.1169. View

17.

Gekko K, Timasheff S . Thermodynamic and kinetic examination of protein stabilization by glycerol. Biochemistry. 1981; 20(16):4677-86. DOI: 10.1021/bi00519a024. View

18.

Asami S, Inoue K, Matsumoto K, Murachi A, Akazawa T . NADP-malic enzyme from maize leaf: purification and properties. Arch Biochem Biophys. 1979; 194(2):503-10. DOI: 10.1016/0003-9861(79)90645-3. View

19.

Walker G, Ku M, Edwards G . Catalytic activity of maize leaf phosphoenolpyruvate carboxylase in relation to oligomerization. Plant Physiol. 1986; 80(4):848-55. PMC: 1075218. DOI: 10.1104/pp.80.4.848. View

20.

Iglesias A, Andreo C . Kinetic and Structural Properties of NADP-Malic Enzyme from Sugarcane Leaves. Plant Physiol. 1990; 92(1):66-72. PMC: 1062249. DOI: 10.1104/pp.92.1.66. View