PMID: 108526Mar 1, 1979

Pyruvate and phosphoenolpyruvate carboxylase in methylotrophs

Mikrobiologiia
N V Loginova, Iu A Trotsenko

Abstract

The activity of pyruvate and phosphoenolpyruvate carboxylases was determined in cell extracts of obligate and facultative methylotrophs which metabolized monocarbon reduced compounds via different pathways. Phosphoenolpyruvate carboxylase was found to be the only enzyme responsible for the high level of CO2 fixation by methylotrophs with the serine pathway (Methylosinus trichosporium, Hyphomicrobium vulgare, Pseudomonas methylica). Methylotrophs with the hexulose phosphate pathway Mehylobacter chroococcum, Methylomonas methanica, Pseudomonas oleovorans, Arthrobacter globiformis) and yeast (Candida methylica) assimilated less CO2 but contained more enzymes involved in arboxylation of phosphoenolpyruvate (phosphoenolpyruvate carboxylase, EG 4.1.1.31; phosphoenolpyruvate carboxykinase, EC 4.1.1.32) or pyruvate (pyruvate carboxylase, EC 6.4.1.1; malic-enzyme, EC 4.1.1.40). Phosphoenolpyruvate carboxytransphosphorylase (EC 4.1.1.38) was not found in any of the studied strains. The properties and the role of carboxylases in the metabolism of methylotrophs are discussed.

Related Concepts

Arthrobacter
Candida utilis
Carboxy-Lyases
Enzyme Activation
Methylococcaceae
Phosphoenolpyruvate Carboxylase
Pseudomonas
Pyruvate Carboxylase

Related Feeds

Biosynthetic Transformations

Biosyntheic transformtions are multi-step, enzyme-catalyzed processes where substrates are converted into more complex products in living organisms. Simple compounds are modified, converted into other compounds, or joined together to form macromolecules. Discover the latest research on biosynthetic transformations here.