Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Studies on the aminotransferases participating in the glycolate metabolism of the alga mougeotia.

Literature DB >> 16662491

Studies on the aminotransferases participating in the glycolate metabolism of the alga mougeotia.

Abstract

Microbodies from Mougeotia spec., Strain 168.80 contain aminotransferases for conversion of glyoxylate to glycine and serine to hydroxypyruvate. Formation of glycine is possible at highest rates with alanine and glutamate as amino donors, whereas for deamination of serine, pyruvate and glyoxylate are the most convenient substrates. A serine hydroxymethyl-transferase was found exclusively in the mitochondrial fraction. There are indications that this enzyme is bound to the mitochondrial membranes. The activities of all transferases are increased under culture conditions stimulating the synthesis of glycolate.

Entities: Chemical Species

Year: 1982 PMID： 16662491 PMCID： PMC1067145 DOI： 10.1104/pp.70.2.340

Source DB: PubMed Journal: Plant Physiol ISSN： 0032-0889 Impact factor: 8.340

10 in total

6 in total

1. Enzymes of beta-Oxidation in Different Types of Algal Microbodies.

Authors: H Stabenau; U Winkler; W Säftel
Journal: Plant Physiol Date: 1984-07 Impact factor: 8.340

2. Subcellular Distribution of Enzymes of Glycolate Metabolism in the Alga Cyanidium caldarium.

Authors: W Gross; H Beevers
Journal: Plant Physiol Date: 1989-07 Impact factor: 8.340

3. Compartmentation of Peroxisomal Enzymes in Algae of the Group of Prasinophyceae : Occurrence of Possible Microbodies without Catalase.

Authors: H Stabenau; U Winkler; W Säftel
Journal: Plant Physiol Date: 1989-06 Impact factor: 8.340

Studies on the aminotransferases participating in the glycolate metabolism of the alga mougeotia.

1. Microbodies from spirogyra: organelles of a filamentous alga similar to leaf peroxisomes.

2. Properties and intramitochondrial localization of serine hydroxymethyltransferase in leaves of higher plants.

3. Protein measurement with the Folin phenol reagent.

4. Aminotransferases in peroxisomes from spinach leaves.

5. Glyoxylate aminotansferases from oat leaves.

6. The localization of glycollate-pathway enzymes in Euglena.

7. Isolation and oxidative properties of intact mitochondria isolated from spinach leaves.

8. Glycolate and glyoxylate metabolism by isolated peroxisomes or chloroplasts.

9. Purification and characterization of serine:glyoxylate aminotransferase from kidney bean (Phaseolus vulgaris).

10. Serine-glyoxylate aminotransferase from kidney bean (Phaseolus vulgaris). II. The reverse reactions.

1. Enzymes of beta-Oxidation in Different Types of Algal Microbodies.

2. Subcellular Distribution of Enzymes of Glycolate Metabolism in the Alga Cyanidium caldarium.

3. Compartmentation of Peroxisomal Enzymes in Algae of the Group of Prasinophyceae : Occurrence of Possible Microbodies without Catalase.

4. Characterization of Peroxisomes from the Alga Bumilleriopsis filiformis.

5. Aminotransfer from Alanine and Glutamate to Glycine and Serine during Photorespiration in Oat Leaves.

6. The presence of glycollate oxidase and dehydrogenase in Dunaliella primolecta.