| Literature DB >> 6069283 |
Abstract
The relative rates of catabolism of glucose and glucose-6-phosphate by intact-cell suspensions of the meningopneumonitis agent, a member of the psittacosis group (Chlamydia), and the properties of the hexokinase and glucose-6-phosphate dehydrogenase of these suspensions were investigated. It is proposed that the hexokinase is a host enzyme bound to the surface of the meningopneumonitis cell and that glucose-6-phosphate is the first substrate in the conversion of hexose to pentose to be attacked by enzymes synthesized by the meningopneumonitis agent.Entities:
Mesh:
Substances:
Year: 1967 PMID: 6069283 PMCID: PMC276746 DOI: 10.1128/jb.94.4.867-869.1967
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490