1996
DOI: 10.1016/s0304-4165(96)00082-7
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Cloning and sequencing of a cluster of genes encoding novel enzymes of trehalose biosynthesis from thermophilic archaebacterium Sulfolobus acidocaldarius

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Cited by 113 publications
(70 citation statements)
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“…The gene products of all0167 and all0168 show 38 % and 45 % identity to Mts and Mth from Sulfolobus acidocaldarius, respectively, which produce trehalose from the reducing end of a-1,4-glucan by sequential reactions (Maruta et al, 1996). The gene product of all0166 shows 32 % identity to trehalase from Saccharomyces cerevisiae, which hydrolyses trehalose (Kopp et al, 1993).…”
Section: Resultsmentioning
confidence: 99%
“…The gene products of all0167 and all0168 show 38 % and 45 % identity to Mts and Mth from Sulfolobus acidocaldarius, respectively, which produce trehalose from the reducing end of a-1,4-glucan by sequential reactions (Maruta et al, 1996). The gene product of all0166 shows 32 % identity to trehalase from Saccharomyces cerevisiae, which hydrolyses trehalose (Kopp et al, 1993).…”
Section: Resultsmentioning
confidence: 99%
“…This pathway is also found in other bacterial species such as Rhizobium (Maruta et al, 1996a), Bradyrhizobium japonicum (Sugawara et al, 2010) and Corynebacterium (Tzvetkov et al, 2003), but is missing in other major bacterial groups including E. coli and Bacillus subtilis. Archaea Sulfolobus also uses this pathway for trehalose synthesis (Maruta et al, 1996b).…”
Section: Trey-trez Pathwaymentioning
confidence: 99%
“…In Sulfolobus acidocaldarius, M. tuberculosis and Arthrobacter sp. Q36 the treY and treZ genes constitute an operon with a third gene designated as treX, which is thought to have a glycogendebranching function in the trehalose biosynthesis process (Maruta et al, 1996c(Maruta et al, , 2000Cole et al, 1998). A possible treX homologue, NCgl2026, was identified in the C. glutamicum genome 10 kb upstream of treY gene (data not shown).…”
Section: Analysis Of C Glutamicum Genome Sequence Datamentioning
confidence: 99%
“…An alternative pathway for trehalose synthesis that uses glycogen as the initial substrate (TreYTreZ pathway; Fig. 1b) was discovered in some bacteria (Maruta et al, 1996a, b) and archaea (Maruta et al, 1996c). In this case, first the terminal a(1R4) glycosidic bond at the reducing end of the a-glucan polymer is transformed into an a(1R1) glycosidic bond via transglycosylation, resulting in the formation of a terminal trehalosyl unit.…”
Section: Introductionmentioning
confidence: 99%