A new enzyme, l-ribose isomerase from Acinetobacter sp. strain DL-28

Shimonishi, Tsuyoshi; Izumori, Ken

doi:10.1016/0922-338x(96)81468-1

Cited by 41 publications

(19 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…strain DL-28 has been used for the reversible isomerization of L-ribose to Lribulose (Shimonishi & Izumori, 1996). However, the enzyme is not stable over 30 u C, which limits the overall process productivity significantly.…”

mentioning

confidence: 99%

Cohnella laeviribosi sp. nov., isolated from a volcanic pond

Cho

Lee

et al. 2007

International Journal of Systematic and Evolutionary Microbiology

View full text Add to dashboard Cite

A novel thermophilic and endospore-forming Gram-positive bacterium capable of assimilating and isomerizing L-ribose was isolated from a volcanic area in Likupang, Indonesia. The isolate, RI-39 T , was able to grow at high temperatures (37-60 6C); optimum growth was observed at pH 6.5 and 45 6C. The strain contained MK-7 (87 %) as the main respiratory quinone and had a DNA G+C content of 51 mol%. The major cellular fatty acids of the isolate were iso-C 16 : 0 and anteiso-C 15 : 0 and the predominant polar lipids were diphosphatidylglycerol, phosphatidylglycerol, phosphatidylethanolamine and lysyl-phosphatidylglycerol. Phylogenetic analysis based on 16S rRNA gene sequences revealed that the isolate represents an evolutionary lineage that is distinct from those of other Cohnella species. Based on morphological, physiological and chemotaxonomic characteristics and 16S rRNA gene sequence comparisons, it is proposed that strain RI-39 T represents a novel species, Cohnella laeviribosi sp. nov. The type strain is RI-39 T (5KCTC 3987 T 5KCCM 10653P T 5CCUG 52217 T ).

show abstract

mentioning

confidence: 99%

Cohnella laeviribosi sp. nov., isolated from a volcanic pond

Cho

Lee

et al. 2007

International Journal of Systematic and Evolutionary Microbiology

View full text Add to dashboard Cite

show abstract

“…For example, Pseudomonas cichorii ST-24 and Acinetobacter sp. strain DL-28, which produce D-tagatose 3-epimerase and L-ribose isomerase, respectively, were isolated from soil and utilized for the preparation of a number of uncommon sugars (1,(16)(17)(18)(19)32). In order to improve the productivity of the sugars, the enzymes were later genetically engineered (14,15,26).…”

mentioning

confidence: 99%

Cloning, Nucleotide Sequence, and Overexpression of the l -Rhamnose Isomerase Gene from Pseudomonas stutzeri in Escherichia coli

Leang

Takada

Ishimura

et al. 2004

Appl Environ Microbiol

Self Cite

View full text Add to dashboard Cite

The gene encoding L-rhamnose isomerase (L-RhI) from Pseudomonas stutzeri was cloned into Escherichia coli and sequenced. A sequence analysis of the DNA responsible for the L-RhI gene revealed an open reading frame of 1,290 bp coding for a protein of 430 amino acid residues with a predicted molecular mass of 46,946 Da. A comparison of the deduced amino acid sequence with sequences in relevant databases indicated that no significant homology has previously been identified. An amino acid sequence alignment, however, suggested that the residues involved in the active site of L-RhI from E. coli are conserved in that from P. stutzeri. The L-RhI gene was then overexpressed in E. coli cells under the control of the T5 promoter. The recombinant clone, E. coli JM109, produced significant levels of L-RhI activity, with a specific activity of 140 U/mg and a volumetric yield of 20,000 U of soluble enzyme per liter of medium. This reflected a 20-fold increase in the volumetric yield compared to the value for the intrinsic yield. The recombinant L-RhI protein was purified to apparent homogeneity on the basis of three-step chromatography. The purified recombinant enzyme showed a single band with an estimated molecular weight of 42,000 in a sodium dodecyl sulfate-polyacrylamide gel. The overall enzymatic properties of the purified recombinant L-RhI protein were the same as those of the authentic one, as the optimal activity was measured at 60°C within a broad pH range from 5.0 to 11.0, with an optimum at pH 9.0.Unusual carbohydrates, simply termed "rare sugars," are referred to as sugars that exist in an extremely scanty amount in nature; they include,tagatose, allitol, and others. Rare sugars have been proven to be of paramount significance not only in food industries but also in pharmaceutical and nutritional industries on account of their multipurpose applications, such as their use as reducedcalorie sweeteners, inhibitors of microbial growth, bulking agents, and memory enhancers (4,(22)(23)(24)(25). Yet the unavailability and scarcity of these uncommon sugars result in their high cost and limitations in usage as starting materials or research reagents. Consequently, there has been a dearth of literature reporting on the mass production of rare sugars. In recent years, however, microbial and enzymatic reactions have become increasingly significant and have played pivotal roles in the production of unusual sugars.We are mainly working on the production and/or mass production of various kinds of rare sugars by using microorganisms screened from a variety of ecological habitats and their enzymes. For example, Pseudomonas cichorii ST-24 and Acinetobacter sp. strain DL-28, which produce D-tagatose 3-epimerase and L-ribose isomerase, respectively, were isolated from soil and utilized for the preparation of a number of uncommon sugars (1,(16)(17)(18)(19)32). In order to improve the productivity of the sugars, the enzymes were later genetically engineered (14,15,26). Furthermore, members of our laboratory recently isolated a mutant s...

show abstract

“…Recently, an L-ribose isomerase (RI) catalyzing the reversible conversion of L-ribulose to L-ribose, as well as the conversion of D-lyxose to D-xylulose, was isolated from Acinetobacter sp. strain DL-28 (30,35). No enzyme of this type was previously known to exist.…”

mentioning

confidence: 96%