Premium
A critical analysis of kinetic data of 3‐hexulosephosphate synthases M ICHAELIS ‐M ENTEN or complex characteristics
Author(s) -
Müller R.,
Babel W.
Publication year - 1980
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.19800200504
Subject(s) - kinetic energy , bacteria , plateau (mathematics) , chemistry , enzyme , arthrobacter , kinetics , methanol , stereochemistry , biochemistry , biology , organic chemistry , physics , mathematics , genetics , mathematical analysis , quantum mechanics
Investigations of the 3‐hexulosephosphate synthase (HPS) from different methylotrophic bacteria have revealed apparent discrepancies in kinetic behaviour. In all methanol‐utilizing species investigated by us the kinetic characteristics showed intermediary plateau regions. Therefore, this behaviour is assumed to be a general feature of the HPS from all non‐methane‐utilizing methylotrophic bacteria. However, this assumption is in contrast to the results of other authors. Both for Methylomonas M15 (S AHM et al. 1976) and Methylomonas aminofaciens 77 a (K ATO et al. 1977, 1978) M ICHAELIS ‐M ENTEN kinetics of the HPS were stated. To check the validity of our assumption we have analyzed the kinetic data given by others. Indications of the existence of intermediary plateau regions could be found with the enzyme from Arthrobacter globiformis (B YKOVSKAYA and V ORONKOV 1977) and Methylomonas aminofaciens 77 a (K ATO et al. 1978). Furthermore, biphasic A RRHENIUS plots indicate a multiple character of the HPS from these species as could already be demonstrated with the enzyme from Bacterium MB 58 and Pseudomonas oleovorans . In addition, causes which may obscure the detection of intermediary plateau regions are demonstrated.