Open AccessPathways of methylacetate metabolism in methylotrophic bacteria
Author(s) -
Rakov D.Y.,
Doroni.V.,
Trotsenko Y.A.,
Alieva R.M.
Publication year - 1990
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.1574-6968.1990.tb13838.x
Subject(s) - biochemistry , formaldehyde dehydrogenase , glyoxylate cycle , nad+ kinase , formate , methanol dehydrogenase , chemistry , pseudomonas , glycolaldehyde , methanol , formaldehyde , citric acid cycle , enzyme , bacteria , metabolism , biology , organic chemistry , genetics , catalysis
10 bacterial strains utilizing methylacetate as a source of carbon and energy were isolated. Two of the most active strains ( Pseudomonas spp. 27RD and 24RA) completely consumed this substrate at a concentration of 0.2% (v/v) during 24 and 36 h, respectively. Both strains possessed non‐specific inducible carboxyl esterase that hydrolyzed methylacetate to methanol and acetate. The latter was then metabolized through the Krebs cycle and glyoxylate shunt. Pseudomonas 27RD had inducible dehydrogenases of methanol (PMS), formaldehyde (NAD) and formate (PMS) as well as hexulosephosphate synthase. The organism assimilated methanol via the ribulose monophosphate cycle (FBP‐variant, TA/TK). Alternatively, Pseudomonas 24RA had no methanol dehydrogenase (PMS or NAD) and enzymes of the RuMP‐ and RuBP‐pathways, but possessed the low alcohol oxidase activity as well as inducible dehydrogenases of formaldehyde (NAD, GSH) and formate (PMS), hydroxypyruvate reductase, serine‐glyoxylate transaminase and malte lyase.