Subcellular localization of two porphyrin-synthesis enzymes in Pisum sativum (pea) and Arum (cuckoo-pint) species.
The subcellular location of the two porphyrin-synthesis enzymes 5-aminolaevulinate dehydratase (ALAD) and porphobilinogen deaminase (PBGD) was investigated in Pisum sativum (pea) leaves and spadices of Arum (cuckoo-pint). Throughout the tissue-fractionation procedures the distribution of the two enzymes paralleled that of the plastid marker enzyme (ADP-glucose pyrophosphorylase), even in Arum, a tissue where the synthesis of non-plastid haem is predominant. The distribution of cytosolic marker enzyme (lactate dehydrogenase) was significantly different from that of ALAD and PBGD and, although purified mitochondria from both species had some residual activity, this was always less than contaminating plastid marker enzyme. The results suggest that ALAD and PBGD are exclusively plastid enzymes. The significance of this for the role of plastids in cellular porphyrin synthesis is discussed.
Smith
A G
AG
Department of Botany, University of Cambridge, U.K.
D000429:Alcohol Oxidoreductases / Q000378:metabolism; D000642:Ammonia-Lyases / Q000378:metabolism*; D002499:Centrifugation, Density Gradient; D007887:Fabaceae / Q000201:enzymology; D011163:Hydroxymethylbilane Synthase / Q000378:metabolism*; D050537:Hydroxypyruvate Reductase; D008291:Malate Dehydrogenase / Q000378:metabolism; D010944:Plants / Q000201:enzymology*; D010946:Plants, Medicinal; D000623:Porphobilinogen Synthase / Q000378:metabolism*; D011166:Porphyrins / Q000096:biosynthesis*; D013347:Subcellular Fractions / Q000201:enzymology; D014357:Trypsin / Q000494:pharmacology
D011166:Porphyrins; D000429:Alcohol Oxidoreductases; D008291:Malate Dehydrogenase; D050537:Hydroxypyruvate Reductase; D011163:Hydroxymethylbilane Synthase; D014357:Trypsin; D000623:Porphobilinogen Synthase; D000642:Ammonia-Lyases