scholarly journals A Cytosolic Bypass and G6P Shunt in Plants Lacking Peroxisomal Hydroxypyruvate Reductase

2019 ◽  
Vol 180 (2) ◽  
pp. 783-792 ◽  
Author(s):  
Jiying Li ◽  
Sarathi M. Weraduwage ◽  
Alyssa L. Preiser ◽  
Stefanie Tietz ◽  
Sean E. Weise ◽  
...  
Keyword(s):  
Hydroxypyruvate Reductase

Crystallization and preliminary diffraction studies of hydroxypyruvate reductase (d-glycerate dehydrogenase) from Hyphomicrobium methylovorum

1992 ◽  
Vol 225 (3) ◽  
pp. 909-911 ◽  
Author(s):  
Jonathan D. Goldberg ◽  
Peter Brick ◽  
Toyokazu Yoshida ◽  
Toshio Mitsunaga ◽  
Takashi Oshiro ◽  
...  
Keyword(s):  
Hydroxypyruvate Reductase

scholarly journals The metabolism of nitrilotriacetate by a pseudomonad

1973 ◽  
Vol 136 (4) ◽  
pp. 1059-1068 ◽  
Author(s):  
Roger E. Cripps ◽  
Ann S. Noble
Keyword(s):  
Oxidative Metabolism ◽  
Sole Source ◽  
Serine Hydroxymethyltransferase ◽  
Glycine Decarboxylase ◽  
Hydroxypyruvate Reductase ◽  
Anaerobic Conversion ◽  
Thiamin Pyrophosphate ◽  
Serine Metabolism ◽  
Successive Removal

1. An organism that grows on nitrilotriacetate as sole source of carbon and energy was isolated in pure culture and was identified as a pseudomonad. 2. Cell-free extracts of the nitrilotriacetate-grown pseudomonad contain an enzyme that catalyses the NADH-and O2-dependent oxidation of nitrilotriacetate to iminodiacetate and glyoxalate. This enzyme is absent from extracts of glucose-grown cells. 3. Compared with growth on glucose, growth on nitrilotriacetate results in increased activities of enzymes of glycine and serine metabolism, namely serine hydroxymethyltransferase, glycine decarboxylase, serine–oxaloacetate aminotransferase and hydroxypyruvate reductase. 4. Cell-free extracts of the nitrilotriacetate-grown organism contain the enzyme glyoxalate carboligase and, when supplemented with NADH, Mg2+and thiamin pyrophosphate, can catalyse the anaerobic conversion of glyoxalate into glycerate. 5. These results are incorporated in a scheme which shows the oxidative metabolism of nitrilotriacetate by the successive removal of C2 units to form 2mol of glyoxalate and 1mol of glycine per mol of nitrilotriacetate degraded. The glyoxalate and glycine are then both metabolized to glycerate by separate pathways, via tartronic semialdehyde and serine respectively. The role of this scheme in the growth of the organism on nitrilotriacetate is discussed.

Inhibition of peroxisomal hydroxypyruvate reductase (HPR1) by tyrosine nitration

2013 ◽  
Vol 1830 (11) ◽  
pp. 4981-4989 ◽  
Author(s):  
Francisco J. Corpas ◽  
Marina Leterrier ◽  
Juan C. Begara-Morales ◽  
Raquel Valderrama ◽  
Mounira Chaki ◽  
...  
Keyword(s):  
Tyrosine Nitration ◽  
Hydroxypyruvate Reductase
Sign in / Sign up

Export Citation Format

Share Document