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B6db references: 20852637

type Journal Article
authors Ramazzina, I.; Costa, R.; Cendron, L.; Berni, R.; Peracchi, A.; Zanotti, G.; Percudani, R.
title An aminotransferase branch point connects purine catabolism to amino acid recycling
journal Nat Chem Biol
Activity pucg
Family pucg
sel selected
ui 20852637
year (2010)
volume 6
pages 801-806
abstract Although amino acids are known precursors of purines, a pathway for the direct recycling of amino acids from purines has never been described at the molecular level. We provide NMR and crystallographic evidence that the PucG protein from Bacillus subtilis catalyzes the transamination between an unstable intermediate ((S)-ureidoglycine) and the end product of purine catabolism (glyoxylate) to yield oxalurate and glycine. This activity enables soil and gut bacteria to use the animal purine waste as a source of carbon and nitrogen. The reaction catalyzed by (S)-ureidoglycine–glyoxylate aminotransferase (UGXT) illustrates a transamination sequence in which the same substrate provides both the amino group donor and, via its spontaneous decay, the amino group acceptor. Structural comparison and mutational analysis suggest a molecular rationale for the functional divergence between UGXT and peroxisomal alanine-glyoxylate aminotransferase, a fundamental enzyme for glyoxylate detoxification in humans.
last changed 2010/10/21 18:02

B6db references