Open AccessAssimilation of methylamine by Paracoccus denitrificans involves formaldehyde transport by a specific carrier
Author(s) -
Köstler Margareta,
Kleiner Diethelm
Publication year - 1989
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1989.tb03587.x
Subject(s) - paracoccus denitrificans , formaldehyde , methylamine , chemistry , formaldehyde dehydrogenase , biochemistry , formate dehydrogenase , enzyme kinetics , formate , medicinal chemistry , enzyme , active site , catalysis , nad+ kinase
Abstract Assimilation of methylamine by Paracoccus denitrificans involves the following enzymes: a periplasmic methylamine dehydrogenase, a formaldehyde transport system, cytoplasmic formaldehyde and formate dehydrogenase. Formaldehyde transport follows saturation kinetics with a high substrate affinity ( K m = 7 μ M), and is severely inhibited by iodoacetate, cyanide and p ‐trifluoromethoxy carbonylcyanide phenylhydrazone. Expression of the formaldehyde carrier is regulated by the carbon source.