一二三四区视频,亚洲少妇熟女色,日本久热无码视频网,欧美国产日韩大尺度,亚洲a视频,久久少妇一区二区,日韩999无码视频,刺激久久久久久久,啊啊啊啊不要啊在线

ChemicalBook >> journal list >> Applied and Environmental Microbiology >>article
Applied and Environmental Microbiology

Applied and Environmental Microbiology

IF: 3.9
Download PDF

Evolution and separation of actinobacterial pyranose and C-glycoside-3-oxidases

Published:24 January 2024 DOI: 10.1128/aem.01676-23 PMID: 38179968
Anja Kostelac,?André Taborda,?Lígia O Martins,?Dietmar Haltrich

Abstract

FAD-dependent pyranose oxidase (POx) and C-glycoside-3-oxidase (CGOx) are both members of the glucose-methanol-choline superfamily of oxidoreductases and belong to the same sequence space. Pyranose oxidases had been studied for their oxidation of monosaccharides such as D-glucose, but recently, a bacterial C-glycoside-3-oxidase that is phylogenetically related to POx and that reacts with C-glycosides such as carminic acid, mangiferin or puerarin has been described. Since these actinobacterial CGOx enzymes belong to the same sequence space as bacterial POx, they must have evolved from the same ancestor. Here, we performed a phylogenetic analysis of actinobacterial sequences and resurrected seven ancestral enzymes of the POx/CGOx sequence space to study the evolutionary trajectory of substrate preferences for monosaccharides and C-glycosides. Clade I, with its dimeric member POx from Kitasatospora aureofaciens, shows strict preference for monosaccharides (D-glucose and D-xylose) and does not react with any of the glycosides tested. No extant member of clade II has been studied to date. The two extant members of clades III and IV, monomeric POx/CGOx from Pseudoarthrobacter siccitolerans and Streptomyces canus, oxidized both monosaccharides as well as various C-glycosides (homoorientin, isovitexin, mangiferin, and puerarin). Steady-state kinetic parameters of several clades III and IV ancestral enzymes indicate that the generalist ancestor N35 slowly evolved to present-day enzymes with a much higher preference for C-glycosides than monosaccharides. Based on structural predictions of ancestors, we hypothesize that the strict specificity of bacterial clade I POx (and also fungal POx) is the result of oligomerization, which in turn results from the evolution of protein segments that were shown to be important for oligomerization, the arm, and the head domain.IMPORTANCEC-Glycosides often form active compounds in various plants. Breakage of the C-C bond in these glycosides to release the aglycone is challenging and proceeds via a two-step reaction, the oxidation of the sugar and subsequent cleavage of the C-C bond. Recently, an enzyme from a soil bacterium, FAD-dependent C-glycoside-3-oxidase (CGOx), was shown to catalyze the initial oxidation reaction. Here, we show that CGOx belongs to the same sequence space as pyranose oxidase (POx), and that an actinobacterial ancestor of the POx/CGOx family evolved into four clades, two of which show a high preference for C-glycosides.

Substances (4)

Materials
Procduct Name CAS Molecular Formula Supplier Price
ISOVITEXIN 38953-85-4 C21H20O10 177 suppliers $11.00-$3655.00
ISOVITEXIN 38953-85-4 C21H20O10 177 suppliers $11.00-$3655.00
ISOVITEXIN 38953-85-4 C21H20O10 177 suppliers $11.00-$3655.00
ISOVITEXIN 38953-85-4 C21H20O10 177 suppliers $11.00-$3655.00

Similar articles

银川市| 禹州市| 屯门区| 河曲县| 龙里县| 新郑市| 大名县| 昭苏县| 庆阳市| 丁青县| 东兴市| 社会| 曲水县| 冀州市| 肥城市| 沧源| 乾安县| 霍邱县| 上蔡县| 汶川县| 梅州市| 舞钢市| 义乌市| 宜章县| 柘城县| 五河县| 兰州市| 荔波县| 兰考县| 滦平县| 乐至县| 康定县| 吴忠市| 天峻县| 锡林郭勒盟| 积石山| 永宁县| 佛山市| 信阳市| 布拖县| 九江市|