Proline oxidase activity

Samuels, S.E., K.S. Acton, and R.O. Ball, 1989. Pyrroline-5-carboxylate reductase and proline oxidase activity in the neonatal pig. J. Nutr. 119, 1999-2004. 

Hamase, K., Inoue, T., Morikawa, A., Konno, R., Zaitsu, K. (2001). Determination of free d-proline and D-leucine in the brains of mutant mice lacking D-amino acid oxidase activity. Anal. Biochem. 298, 253-258. 

Fig. I. Metabolic map for synthesis and metabolism of glutamate and aspartate. AAT = aspartate aminotransferase AS = asparagine synthetase GAD = glutamic acid decarboxylase GDH = glutamate dehydrogenase GS = glutamine synthetase OAT = ornithine D-aminotransferase P5CDH = l-pyrroline-5-carboxylate dehydrogena.se PAG = phosphate-activated glutaminase PO = proline oxidase TCA = tricarboxylic acid.

Pig-6 Proline oxidase homolog Transcriptional activation Apoptosis Polyak etal. (1997)... 

More recently we have studied the effects of j3-thia-proline on protein synthesizing systems(56). -Thiapro-line,first synthesized by Eourneau et al. (57) ilia-S not been assayed in biological systems. We have obtained preliminary data indicating that it is a substrate for hog kidney D-aminoacid oxidase and for rat liver mitochondria proline oxidase,two enzymes active on y-thiaproline. 

The a-ketoacid-dependent enzymes are distinguished from other non-haem iron enzymes by their absolute requirement for an a-ketoacid cofactor as well as Fe(II) and O2 for activity. They catalyse two types of reaction (Table 2.3), hydroxyla-tion and oxidation. In both, the a-ketoglutarate is decarboxylated and one oxygen atom introduced into the succinate formed in the hydroxylases, the other oxygen atom is introduced into the substrate, while in the oxidases it is found in water, together with the cyclized product. In general these enzymes require one equivalent of Fe(II) an a-ketoacid, usually a-ketoglutarate and ascorbate. Examples of these enzymes include proline 4-hydroxylase, prolyl and lysyl hydroxylase, which... 

More recently Huang and Cavalieri (1979) have studied a similar enzyme in mitochondria isolated from spinach leaves. This enzyme had a pH optimum at 8.0-8.5 with a A , for proline of 28 mAf. The enzyme was linked to the mitochondrial electron transport system and MgCl2 and flavin adenine dinucleotide were required for maximal activity. The spinach oxidase also was inactive after Triton X-100 treatment. 

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