Oligo-l,6-glucosidase

T. Nagayama, A strong correlation between the increase in number of proline residues and the rise in thermostability of five Bacillus oligo-l,6-glucosidases, Appl. Microbiol. Biotechnd. 1987, 26, 546—551. 

K. Watanabe, T. Masuda, H. Ohashi, H. Mi-hara, Y. Suzuki, Multiple proline substitutions cumulatively thermostabilize Bacillus cereus ATCC7064 oligo-l,6-glucosidase. Irrefragable proof supporting the proline rule, Eur.J. Biochem. 1994, 226(2), 277-283. 

Y. Suzuki, Proline residues responsible for thermostability occur with high frequency in the loop regions of an extremely thermostable oligo-l,6-glucosidase from Bacillus thermoglucosidasius KP1006,J. Biol. Chem. 1991, 266(36), 24287-24294. 

K. Watanabe, Y. Hata, H. Kizaki, Y Katsube, Y. Suzuki, The refined crystal structure of Bacillus cereus oligo-l,6-glucosidase at 2.0 A resolution structural characterization of proline-substitution sites for protein thermostabilization, J. Mol. Biol. 1997, 269(1), 142-153. 

Oligo-l,6-glucosidase Isomaltase Dextrin 6-a-glucanohydrolase 3.2.1.10 Small intestine Dextrins... 

Amino-acid sequences around the essential carboxylic acid group in the active sites of the sucrose a-D-glucohydrolase oligo-l,6-glucosidase (sucrase-isomaltase) complex of rabbit small intestines have been determined by selective labelling with [ H]conduritol-B epoxide. ... 

Brown DH, Brown BI (1966) Enzymes of glycogen debranching amylo-l,6-glucosidase and oligo-l,4->l,4-glucantransferase. Methods Enzymol 8 515-524... 

Mortimer and Hawthorne165 and Barnett4 summarized work on the complex, genetical control of a-D-glucosidase and oligo-(l— 6)-D-glu-... 

Studies on the enzyme complex oligo-l,6-D-glucosidase-sucrose a-D-glucohydro-lase ( sucrase-isomaltase ) of the AB intestinal brush border membrane have shown that a hydrophobic section of the oligo-l,6-D-glucosidase is responsible for binding of the complex to the membrane (see p. 522). ... 

The concurrent action of sucrose a-D-glucohydrolase and oligo-l,6-D-gluco-sidase active sites of the hybrid oligo-l,6-D-glucosidase-sucrose a-D-glucohydrolase ( sucrose-isomaltase ) from rat intestine on an a-limit dextrin was studied by use of 6 -maltotriosylmaltotriose isolated from the products of controlled action of pullulanase on pullulan (see p. 522). ... 

The selective solubilization of a-D-glucosidases from the complex mixture of such enzymes in porcine intestinal mucosa led to the conclusion that separate enzymes are involved in the hydrolysis of isomaltose and the a-limit dextrins formed from starch by a-amylase ( isomaltase and limit dextrinase respectively). Various aspects of the enzymology of oligo-l,6-D-glucosidase (limit dextrinase ) from peas have been reported. ... 

The levels of -D-galactosidase have been measured in jejunal biopsy specimens from normals and from sibling cases involving a deficiency of sucrose -d-glucohydrolase-oligo-l,6-D-glucosidase ( sucrase-isomaltase ). ... 

Oligo-(1 - 6)-D-glucosidases Various aspects of the enzymology of oligo-(l dextrinase ) from peas have been reported. ... 

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