Catalytic properties of d-xylose isomerase from Streptomyces violaceoruber

Callens, Mia; Kersters-Hilderson, H; Opstal, Omer Van; Bruyne, Clement K. De

doi:10.1016/0141-0229(86)90069-4

Cited by 69 publications

(53 citation statements)

References 18 publications

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“…A qualitative measure of xylose isomerase activity was achieved using permeabilized, induced E. coli cells, as described (15). A coupled assay linked to sorbitol dehydrogenase was used for quantitative measures of activity (16). The reaction mixture contained 10 units of sorbitol dehydrogenase (Boehringer Mannheim), 10 mM MnC12, 5 mM NADH, and D-xylose (mutarotated) in 10 mM triethanolamine buffer (pH 7.2).…”

Section: Methodsmentioning

confidence: 99%

Identification of essential histidine residues in the active site of Escherichia coli xylose (glucose) isomerase.

Batt

Jamieson

Vandeyar

1990

Proc. Natl. Acad. Sci. U.S.A.

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Section: Methodsmentioning

confidence: 99%

Identification of essential histidine residues in the active site of Escherichia coli xylose (glucose) isomerase.

Batt

Jamieson

Vandeyar

1990

Proc. Natl. Acad. Sci. U.S.A.

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“…XI activity was assayed in two steps (5). This assay is different from the one used previously (37), with the following modifications: crude cell extract was mixed in 700 mM xylose, 10 mM MnCl 2 , and 100 mM triethanolamine in a total volume of 500 l. XI in the crude extract was allowed to convert xylose to xylulose for 10 min at 60°C.…”

mentioning

confidence: 99%

Deletion of the GRE3 Aldose Reductase Gene and Its Influence on Xylose Metabolism in Recombinant Strains of Saccharomyces cerevisiae Expressing the xylA and XKS1 Genes

Träff

Cordero

Zyl

et al. 2001

Appl Environ Microbiol

142

111

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Saccharomyces cerevisiae ferments hexoses efficiently but is unable to ferment xylose. When the bacterial enzyme xylose isomerase (XI) from Thermus thermophilus was produced in S. cerevisiae, xylose utilization and ethanol formation were demonstrated. In addition, xylitol and acetate were formed. An unspecific aldose reductase (AR) capable of reducing xylose to xylitol has been identified in S. cerevisiae. The GRE3 gene, encoding the AR enzyme, was deleted in S. cerevisiae CEN.PK2-1C, yielding YUSM1009a. XI from T. thermophilus was produced, and endogenous xylulokinase from S. cerevisiae was overproduced in S. cerevisiae CEN.PK2-1C and YUSM1009a. In recombinant strains from which the GRE3 gene was deleted, xylitol formation decreased twofold. Deletion of the GRE3 gene combined with expression of the xylA gene from T. thermophilus on a replicative plasmid generated recombinant xylose utilizing S. cerevisiae strain TMB3102, which produced ethanol from xylose with a yield of 0.28 mmol of C from ethanol/mmol of C from xylose. None of the recombinant strains grew on xylose.

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“…Furthermore Sanchez and Smiley [14], Takasaki [18] and Kasumi et al [19] have recognized a stabilization effect of the tetrameric structure by the cations mentioned. In consistence with these results, Callens et al [17] demonstrated that Co2+ is superior to Mg2+ as a protector against thermal denaturation.…”

Section: Enzyme D-xylose Isomerase (Ec 531 S)mentioning

confidence: 77%

“…Kasumi et al [23] reported for the Xyl isomerase of S. griseofuscus an M , 180000, that of S. violuceoruber has an M , of 171 700 [24]. From the amino acid composition, derived from the DNA sequence, an M , of 42925 for the monomer has been computed.…”

Section: Resultsmentioning

confidence: 99%

Spectroscopic studies on the metal‐ion‐binding sites of Co²⁺‐substituted D‐xylose isomerase from Streptomyces rubiginosus

Sudfeldt

Schäffer

Kägi

et al. 1990

European Journal of Biochemistry

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The coordination sphere of the two metal-binding sites/subunit of the homotetrameric D-XylOSe isomerase from Streptomyces rubiginosus has been probed by the investigation of the Co2+-substituted enzyme using electronic absorption, CD and magnetic circular dichroic spectroscopies in the visible region. The spectrum of the high-affinity site (B site) has an absorption coefficient, E~~~, of 18 M-' cm-', indicating a distorted octahedral complex geometry. The spectrum of the low-affinity site (A site) shows two absorption maxima at 505 nm and 586 nm with E values of 170 M-' cm-' and 240 M-' cm-', respectively, which indicates a distorted tetrahedral or pentacoordinated complex structure as also observed for the enzyme from Streptomyces violaceoruber [Callens et al. (1988) Biochem. J . 250, 285-2901 having the same feature but lower c values. The first 4 mol Co2+ added/ mol apoenzyme occupy both sites nearly equally. Subsequently the Co2+ located in the A site slowly moves into the B site. After equilibrium is reached, the next 4 mol Co2+/mol again occupy the A site with its typical spectrum, restoring full activity. Addition of 4 mol Cd2+ or Pb2+/mol Co4-loaded derivative displaces the Co2+ from the B site to form the Pb4/Co4 derivative containing Co2+ in the A site, reducing activity fourfold while the Pb4/Pb4 species is completely inactive. In contrast, Eu3+ displaces Co2 ' preferentially from the A site. Thus, the highand low-affinity sites may be different for different cations. After addition of the substrates D-xylose, D-glucose and D-fructose and the inhibitor xylitol the intense Co2+ A-site spectrum of both the active C04/c04 derivative and the less active Pb4/Co4 derivative decreases, indicating that these compounds are bound to the A site, changing the distorted tetrahedral or pentacoordinated symmetry there to a distorted octahedral complex geometry.The intracellular enzyme D-XylOSe isomerase is widely distributed among microorganisms like Streptomyces, Arthrohacter and Bacillus species or other bacteria [l, 21. It catalyzes in vivo the reversible isomerization of u-xylose to D-xylulose in order to utilize D-xylose from xylans as an energy source. In 1957 Marshall and Kooi [3] found that D-xylose isomerase also converts a-D-glucose into a-D-fructose. These stereospecific reactions are of industrial interest for the production of high-fructose corn syrup from starch [4] and for the conversion of hemicellulose to ethanol [5].D-Xylose isomerases from Streptomyces species exist as tetramers consisting of four identical subunits. The evaluation of X-ray crystal structures of Xyl isomerase from S. rubiginosus ATCC 21 175 [6, 71, S. olivochromogenes [8, 91 and S. rubiginosus ATCC 21 132 (previously classified as S. albus) [lo] has shown that the tetramer appears to be a dimer of dimers. This was also found for the Arthrobacter enzyme [l 11. Callens et al. [12] have shown by SDSjPAGE that treatment of the enzyme from S. violaceovuber with 0.1% SDS causes reversible dissociation into active dimers, whereas t...

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Catalytic properties of d-xylose isomerase from Streptomyces violaceoruber

Cited by 69 publications

References 18 publications

Identification of essential histidine residues in the active site of Escherichia coli xylose (glucose) isomerase.

Identification of essential histidine residues in the active site of Escherichia coli xylose (glucose) isomerase.

Deletion of the GRE3 Aldose Reductase Gene and Its Influence on Xylose Metabolism in Recombinant Strains of Saccharomyces cerevisiae Expressing the xylA and XKS1 Genes

Spectroscopic studies on the metal‐ion‐binding sites of Co²⁺‐substituted D‐xylose isomerase from Streptomyces rubiginosus

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Catalytic properties of d-xylose isomerase from Streptomyces violaceoruber

Cited by 69 publications

References 18 publications

Identification of essential histidine residues in the active site of Escherichia coli xylose (glucose) isomerase.

Identification of essential histidine residues in the active site of Escherichia coli xylose (glucose) isomerase.

Deletion of the GRE3 Aldose Reductase Gene and Its Influence on Xylose Metabolism in Recombinant Strains of Saccharomyces cerevisiae Expressing the xylA and XKS1 Genes

Spectroscopic studies on the metal‐ion‐binding sites of Co2+‐substituted D‐xylose isomerase from Streptomyces rubiginosus

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Spectroscopic studies on the metal‐ion‐binding sites of Co²⁺‐substituted D‐xylose isomerase from Streptomyces rubiginosus