Abstract
D-Enzyme, a transglycosylase from potato, has been found to transfer maltodextrin residues from starch to l-sorbose or methyl α-l-sorboside, as well as to d-glucose. Oligosaccharides terminated in l-sorbose or methyl α-l-sorboside are thereby formed. These have been isolated and found to contain α-maltosyl, α-maltotriosyl groups, etc., linked to C-3 of the sorbose or sorboside. The inability of D-enzyme to distinguish between l-sorbose and d-glucose as substrates results from the structural similarity between the two sugars, in particular the equivalence of the C-3 hydroxyl of sorbose, the site of reaction, with the C-4 hydroxyl of glucose. α-Amylase, β-amylase, and starch phosphorylase are likewise unable to differentiate between the two monosaccharides since they attack the sorbose- and sorboside-terminated oligosaccharides in the same way as the corresponding glucose-terminated polymers (maltodextrins).
| Original language | English |
|---|---|
| Pages (from-to) | 592-598 |
| Number of pages | 7 |
| Journal | Archives of Biochemistry and Biophysics |
| Volume | 112 |
| Issue number | 3 |
| State | Published - Dec 1 1965 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Molecular Biology
- Biophysics
- Biochemistry
Cite this
Mechanism of carbohydrase action. XII. l-Sorbose as an acceptor substrate in transfer reactions catalyzed by potato D-enzyme. / Abdullah, M.; Whelan, William J.
In: Archives of Biochemistry and Biophysics, Vol. 112, No. 3, 01.12.1965, p. 592-598.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Mechanism of carbohydrase action. XII. l-Sorbose as an acceptor substrate in transfer reactions catalyzed by potato D-enzyme
AU - Abdullah, M.
AU - Whelan, William J.
PY - 1965/12/1
Y1 - 1965/12/1
N2 - D-Enzyme, a transglycosylase from potato, has been found to transfer maltodextrin residues from starch to l-sorbose or methyl α-l-sorboside, as well as to d-glucose. Oligosaccharides terminated in l-sorbose or methyl α-l-sorboside are thereby formed. These have been isolated and found to contain α-maltosyl, α-maltotriosyl groups, etc., linked to C-3 of the sorbose or sorboside. The inability of D-enzyme to distinguish between l-sorbose and d-glucose as substrates results from the structural similarity between the two sugars, in particular the equivalence of the C-3 hydroxyl of sorbose, the site of reaction, with the C-4 hydroxyl of glucose. α-Amylase, β-amylase, and starch phosphorylase are likewise unable to differentiate between the two monosaccharides since they attack the sorbose- and sorboside-terminated oligosaccharides in the same way as the corresponding glucose-terminated polymers (maltodextrins).
AB - D-Enzyme, a transglycosylase from potato, has been found to transfer maltodextrin residues from starch to l-sorbose or methyl α-l-sorboside, as well as to d-glucose. Oligosaccharides terminated in l-sorbose or methyl α-l-sorboside are thereby formed. These have been isolated and found to contain α-maltosyl, α-maltotriosyl groups, etc., linked to C-3 of the sorbose or sorboside. The inability of D-enzyme to distinguish between l-sorbose and d-glucose as substrates results from the structural similarity between the two sugars, in particular the equivalence of the C-3 hydroxyl of sorbose, the site of reaction, with the C-4 hydroxyl of glucose. α-Amylase, β-amylase, and starch phosphorylase are likewise unable to differentiate between the two monosaccharides since they attack the sorbose- and sorboside-terminated oligosaccharides in the same way as the corresponding glucose-terminated polymers (maltodextrins).
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M3 - Article
C2 - 4286498
AN - SCOPUS:0013825451
VL - 112
SP - 592
EP - 598
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
SN - 0003-9861
IS - 3
ER -