A GH13 glycoside phosphorylase with unknown substrate specificity from Corallococcus coralloides
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چکیده
منابع مشابه
Substrate specificity of 5'-methylthioadenosine phosphorylase from human prostate.
5'-Methylthioadenosine phosphorylase was purified approx. 340-fold from human prostate by using affinity chromatography by Hg-coupled Sepharose. The enzyme, responsible for the breakdown of 5'-methylthioadenosine into adenine and methylthioribose 1-phosphate, was partially characterized. The apparent Km for 5'-methylthioadenosine is 25 microM. It is activated by thiols and shows an absolute req...
متن کاملComplete genome sequence of the fruiting myxobacterium Corallococcus coralloides DSM 2259.
Corallococcus coralloides, like most other myxobacteria, undergoes a developmental program culminating in the formation of fruiting bodies. C. coralloides fruiting bodies are morphologically distinct from those of other fruiting myxobacteria for which full-length genome sequences are available. The genome sequence of the 10.0-Mb C. coralloides genome is presented herein.
متن کاملSubstrate Specificity and Induction of Thymidine Phosphorylase in Escherichia coZi*
Purified preparations from Escherichia coli of the enzyme thymidine :orthophosphate deoxyribosyltransferase (EC 2.4. 2.4) or thymidine phosphorylase are specific for deoxyribose lphosphate. A number of pyrimidine bases function in the reaction, however, including uracil, 5-bromoand 5-aminouracil, 2-thiothymine, and 2-thiouracil, whereas deoxycytidine is inert (1). The level of enzyme in extract...
متن کاملSubstrate Specificity and Induction of Thymidine Phosphorylase in Escherichia Coli.
Purified preparations from Escherichia coli of the enzyme thymidine :orthophosphate deoxyribosyltransferase (EC 2.4. 2.4) or thymidine phosphorylase are specific for deoxyribose lphosphate. A number of pyrimidine bases function in the reaction, however, including uracil, 5-bromoand 5-aminouracil, 2-thiothymine, and 2-thiouracil, whereas deoxycytidine is inert (1). The level of enzyme in extract...
متن کاملMechanistic insight into the substrate specificity of 1,2-β-oligoglucan phosphorylase from Lachnoclostridium phytofermentans
Glycoside phosphorylases catalyze the phosphorolysis of oligosaccharides into sugar phosphates. Recently, we found a novel phosphorylase acting on β-1,2-glucooligosaccharides with degrees of polymerization of 3 or more (1,2-β-oligoglucan phosphorylase, SOGP) in glycoside hydrolase family (GH) 94. Here, we characterized SOGP from Lachnoclostridium phytofermentans (LpSOGP) and determined its crys...
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ژورنال
عنوان ژورنال: Amylase
سال: 2019
ISSN: 2450-9728
DOI: 10.1515/amylase-2019-0003