Premium
Regulation der PEP‐Carboxylase des fakultativ methylotrophen Acetobacter sp. MB 58
Author(s) -
Loffhagen N.,
Babel W.
Publication year - 1982
Publication title -
zeitschrift für allgemeine mikrobiologie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0044-2208
DOI - 10.1002/jobm.19820220705
Subject(s) - pyruvate carboxylase , anabolism , biochemistry , glycolysis , chemistry , energy charge , pyruvate kinase , kinase , enzyme , adenylate kinase
Acetobacter sp. MB 58 assimilates methanol via the fructose‐1,6‐bisphosphate variant of the hexulose phosphate pathway. Glyceraldehyde‐3‐phosphate originates as net product of an assimilation loop involving the regeneration of the C 1 ‐acceptor ribulose‐5‐phosphate and must be available for the de novo synthesis of the C 1 ‐acceptor as well as for the oxidative glycolysis. It is made probable in a regulatory model that this is accomplished via alternating anabolic and catabolic phases which are controlled by concerted action of PEP‐carboxylase and pyruvate kinase. Whereas Ac‐CoA is a crucial effector and ä‐ketoglutarate and aspartate are inhibitors for the PEP‐carboxylase, the pyruvate kinase is assumed to be regulated by energy charge.