Data for RPSD was compiled from protein sequences with experimental support of existence from SwissProt, MetaCyc, and BRENDA.' (2015).ĮPPMN17: 'The functional annotation of protein sequences was performed by the PMN Ensemble Enzyme Prediction Pipeline (E2P2, version 3.1). The training of E2P2 and the reference databases used in the annotation process are based on the Reference Protein Sequence Dataset (RPSD) 3.0. E2P2 annotates protein sequences using homology transfer by integrating both single sequence (BLAST, E-value cutoff = 0.5) where the weight of each predicted model was determined via a 5-by-3 nested cross-validation routine. PMID: 19807880ĮPPMN15: 'The functional annotation of protein sequences was performed by the PMN Ensemble Enzyme Prediction Pipeline (E2P2, version 3.0). 'C acid decarboxylases required for C photosynthesis are active in the mid-vein of the C species Arabidopsis thaliana, and are important in sugar and amino acid metabolism.' Plant J 61(1) 122-33. PMID: 9774405īrown10: Brown NJ, Palmer BG, Stanley S, Hajaji H, Janacek SH, Astley HM, Parsley K, Kajala K, Quick WP, Trenkamp S, Fernie AR, Maurino VG, Hibberd JM (2010). 'A novel, non-redox-regulated NAD-dependent malate dehydrogenase from chloroplasts of Arabidopsis thaliana L.' J Biol Chem 273(43) 27927-33. Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathwayīerkemeyer98: Berkemeyer M, Scheibe R, Ocheretina O (1998). 'Isolated durum wheat and potato cell mitochondria oxidize externally added NADH mostly via the malate/oxaloacetate shuttle with a rate that depends on the carrier-mediated transport.' Plant Physiol 133(4) 2029-39. Pastore03a: Pastore D, Di Pede S, Passarella S (2003). Activation by pyruvate, hydroxypyruvate and glyoxylate and physiological role.' Plant Cell Physiol 42(12) 1373-82. 'Alternative oxidase in durum wheat mitochondria. Pastore01: Pastore D, Trono D, Laus MN, Di Fonzo N, Passarella S (2001). 'Characterization of a cytosolic malate dehydrogenase cDNA which encodes an isozyme toward oxaloacetate reduction in wheat.' Biochimie 86(8) 509-18. It was shown that in the wheat or potato mitochondria, at low physiological NADH concentrations, the malate/oxaloacetate shuttle operated at a high efficiency, with a rate limited by the oxaloacetate/malate antiporter, whereas the presence of either malate/aspartate or G3P shuttle was not observed.ĭing04: Ding Y, Ma QH (2004). The existing of such a shuttle has been reported in wheat and potato In this way, NADH is transferred from cytosol into mitochondria. Oxaloacetate is transported back to the cytosol by the oxaloacetate/malate antiporter. Inside the mitochondrion, malate is oxidized by NAD+ back to oxaloacetate forming NADH. Malate is then transported into the mitochondrial matrix via an oxaloacetate/malate antiporter. In the cytosol, oxaloacetate is reduced to malate by electrons from NADH.

, an oxaloacetate/malate antiporter in the mitochondrial membrane This pathway transports reducing equivalent (NAD/NADH) between the cytosol and the mitochondrion, and involves a cytosolic malate dehydrogenase (MDH) Malate/aspartate shuttle, and the malate/oxaloacetate shuttle (depicted here). Several shuttles exit in cells to transfer and balance reducing equivalents, NAD(P)/NAD(P)H, between different subcellular locations where the reducing equivalents are necessary for different metabolism to continue. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Malate oxaloacetate shuttle