scholarly journals Identification of the Specific Interactors of the Human Lariat RNA Debranching Enzyme 1 Protein

2015 ◽  
Vol 16 (2) ◽  
pp. 3705-3721 ◽  
Author(s):  
So Masaki ◽  
Rei Yoshimoto ◽  
Daisuke Kaida ◽  
Asuka Hata ◽  
Takayuki Satoh ◽  
...  
Keyword(s):  
Debranching Enzyme ◽  
Lariat Rna

scholarly journals Structural basis of lariat RNA recognition by the intron debranching enzyme Dbr1

2014 ◽  
Vol 42 (16) ◽  
pp. 10845-10855 ◽  
Author(s):  
Eric J. Montemayor ◽  
Adam Katolik ◽  
Nathaniel E. Clark ◽  
Alexander B. Taylor ◽  
Jonathan P. Schuermann ◽  
...  
Keyword(s):  
Structural Basis ◽  
Rna Recognition ◽  
Debranching Enzyme ◽  
Lariat Rna

Debranching enzyme from rabbit skeletal muscle; Evidence for the location of two active centres on a single polypeptide chain

FEBS Letters ◽  
1975 ◽  
Vol 58 (1-2) ◽  
pp. 181-185 ◽  
Author(s):  
Edna J. Bates ◽  
Gillian M. Heaton ◽  
Carol Taylor ◽  
John C. Kernohan ◽  
Philip Cohen
Keyword(s):  
Skeletal Muscle ◽  
Polypeptide Chain ◽  
Rabbit Skeletal Muscle ◽  
Debranching Enzyme ◽  
Single Polypeptide Chain ◽  
Single Polypeptide ◽  
Active Centres

scholarly journals A novel alpha-glucosidase from the moss Scopelophila cataractae.

2007 ◽  
Vol 54 (2) ◽  
pp. 401-406 ◽  
Author(s):  
Yoshiki Yamasaki ◽  
Susumu Nakashima ◽  
Haruyoshi Konno
Keyword(s):  
Phosphate Buffer ◽  
Soluble Starch ◽  
Ms Medium ◽  
Starch Digestion ◽  
Soluble Extract ◽  
Debranching Enzyme ◽  
Successive Extraction ◽  
Isoelectric Points ◽  
Alpha Amylase Inhibitor ◽  
Alpha Glucosidase

Scopelophila cataractae is a rare moss that grows on copper-containing soils. S. cataractae protonema was grown on basal MS medium containing copper. A starch-degrading activity was detected in homogenates of the protonema, after successive extraction with phosphate buffer and buffer containing 3 M LiCl. Buffer-soluble extract (BS) and LiCl-soluble extract (LS) readily hydrolyzed amylopectin to liberate only glucose, which shows that alpha-glucosidase (EC 3.2.1.20) in BS and LS hydrolyzed amylopectin. The K(m) value of BS for maltose was 0.427. The K(m) value of BS for malto-oligosaccharide decreased with an increase in the molecular mass of the substrate. The value for maltohexaose was 0.106, which is about four-fold lower than that for maltose. BS was divided into two fractions of alpha-glucosidase (BS-1 and BS-2) by isoelectric focusing. The isoelectric points of these two enzymes were determined to be 4.36 (BS-1) and 5.25 (BS-2) by analytical gel electrofocusing. The two enzymes readily hydrolyzed malto-oligosaccharides. The two enzymes also hydrolyzed amylose, amylopectin and soluble starch at a rate similar to that with maltose. The two enzymes readily hydrolyzed panose to liberate glucose and maltose (1 : 1), and the K(m) value of BS for panose was similar to that for maltotriose, whereas the enzymes hydrolyzed isomaltose only weakly. With regard to substrate specificity, the two enzymes in BS are novel alpha-glucosidases. The two enzymes also hydrolyzed beta-limit dextrin, which has many alpha-1,6-glucosidic linkages near the non-reducing ends, more strongly than maltose, which shows that they do not need a debranching enzyme for starch digestion. The starch-degrading activity of BS was not inhibited by p-chloromercuribenzoic acid or alpha-amylase inhibitor. When amylopectin was treated with BS and LS in phosphate buffer, pH 6.0, glucose, but not glucose-1-phosphate, was detected, showing that the extracts did not contain phosphorylase but did contain an alpha-glucosidase. These results show that alpha-glucosidases should be capable of complete starch digestion by themselves in cells of S. cataractae.

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