NDLI: Identification and characterization of 3,6-anhydro-L-galactose dehydrogenases belonging to the aldehyde dehydrogenase superfamily from marine and soil microorganisms

Content Provider	Springer Nature Link
Author	Cho, Sun Ja Lee, Sun Bok
Copyright Year	2014
Abstract	The complete hydrolysis of agarose produces its monomeric sugars, D-galactose and 3,6-anhydro-Lgalactose (L-AnG). Although enzymes of D-galactose metabolism are well characterized, those involved in L-AnG metabolism have not yet been investigated. In this study, we report the identification and characterization of L-AnG dehydrogenase (L-AnGDH), an aldehyde dehydrogenase (ALDH), catalyzing the first step of L-AnG degradation. To compare substrate and cofactor specificities of L-AnGDH, two L-AnGDH genes obtained from the marine bacterium Postechiella marina (Pm_L-AnGDH) and the soil bacterium Streptomyces coelicolor (Sc_L-AnGDH) were cloned and expressed in E. coli. Whereas the recombinant Pm_LAnGDH and Sc_L-AnGDH were similar in their oligomeric state (homotetramer) and optimum reaction conditions (30℃, pH 8.0), the two enzymes were distinguishable by their substrate and cofactor specificities. Sc_L-AnGDH catalyzed the oxidation of L-AnG using both NAD$^{+}$ and NADP$^{+}$, with a preference for NAD$^{+}$. It also catalyzed the dehydrogenation of L-glyceraldehyde, glycolaldehyde, and L-lactaldehyde in the presence of NAD$^{+}$. On the other hand, Pm_L-AnGDH showed exclusive selectivity towards NADP$^{+}$ and did not oxidize aldehydes other than L-AnG and L-glyceraldehyde. The phylogenetic analysis of amino sequences indicated that L-AnGDH belongs to a novel subfamily within the ALDH superfamily. To our knowledge, this is the first report on the characterization of L-AnGDH.
Starting Page	1058
Ending Page	1068
Page Count	11
File Format	PDF
ISSN	12268372
Journal	Biotechnology and Bioprocess Engineering
Volume Number	19
Issue Number	6
e-ISSN	19763816
Language	English
Publisher	The Korean Society for Biotechnology and Bioengineering
Publisher Date	2015-01-16
Publisher Place	Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	3,6-anhydro-L-galactose dehydrogenase aldehyde dehydrogenase superfamily cofactor specificity agarose metabolism Biotechnology Industrial and Production Engineering
Content Type	Text
Resource Type	Article
Subject	Bioengineering Biomedical Engineering Applied Microbiology and Biotechnology Biotechnology

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