Query
Condition Concatenation Type Data Entry Comparison Numerics Sentence Range Exact Match? Case Sensitive? Literatures Fields
0 && keyword AMY1A > 0 sentence no no oryza body, title, abstract


13 matches found in 4 documents. Results sorted by score (hits) .
Score: 6.00
Title: Functional roles of protein domains on rice alpha-amylase activity .
Author: Terashima M Hosono M Katoh S
Journal: Appl . Microbiol . Biotechnol . Citation: V : 47 ( 4 ) P : 364-7 Year: 1997 Type: ARTICLE
Literature: oryza Field: abstract Doc ID: pub9163949 Accession (PMID): 9163949
Abstract: Characteristics of two rice alpha-amylases Amy1A and Amy3D , and those of two chimeric enzymes Amy1A/3D and Amy3D/1A , engineered from the two isozymes , were compared in the light of the functional roles of protein domains in alpha-amylase . The enzymes that have an Amy1A-type N-terminal domain , Amy1A and Amy1A/3D , showed high activity against soluble starch , while the enzymes that have an Amy3D-type barrel structure , Amy3D and Amy1A/3D , showed high activity in oligosaccharide hydrolysis . Rigidity of protein folding also significantly affected the enzyme activity in both soluble starch and oligosaccharide hydrolysis . Thus , the present work suggests that the structure of the N-terminal domain is important for stability and soluble starch hydrolysis , while the barrel structure that forms the active site significantly affects enzyme activities in oligosaccharide degradation . We have already characterized two rice alpha-amylase isozymes , Amy1A and Amy3D , and a chimeric enzyme engineered from these two isozymes , Amy1A/3D ( Terashima et al 1995 , 1996a , b ) . In spite of the high homology ( 70% ) of their amino acid sequences , Amy1A and Amy3D showed distinct differences in their enzymatic characteristics . The chimeric enzyme Amy1A/3D , which consists of an Amy1A-type N-terminal domain and an Amy3D-type barrel structure , inherited enzymatic characteristics from the both isozymes . In this work , one other chimeric enzyme , Amy3D/1A , which is the counterpart of Amy1A/3D , has been characterized . The characteristics of these four enzymes are discussed in the light of the functional roles of protein domains .
Matching Sentences:
[ Sen. 2, subscore: 2.00 ]: The enzymes that have an Amy1A-type N-terminal domain , Amy1A and Amy1A/3D , showed high activity against soluble starch , while the enzymes that have an Amy3D-type barrel structure , Amy3D and Amy1A/3D , showed high activity in oligosaccharide hydrolysis .
[ Sen. 1, subscore: 1.00 ]: Characteristics of two rice alpha-amylases Amy1A and Amy3D , and those of two chimeric enzymes Amy1A/3D and Amy3D/1A , engineered from the two isozymes , were compared in the light of the functional roles of protein domains in alpha-amylase .
[ Sen. 5, subscore: 1.00 ]: We have already characterized two rice alpha-amylase isozymes , Amy1A and Amy3D , and a chimeric enzyme engineered from these two isozymes , Amy1A/3D ( Terashima et al 1995 , 1996a , b ) .
[ Sen. 6, subscore: 1.00 ]: In spite of the high homology ( 70% ) of their amino acid sequences , Amy1A and Amy3D showed distinct differences in their enzymatic characteristics .
[ Sen. 7, subscore: 1.00 ]: The chimeric enzyme Amy1A/3D , which consists of an Amy1A-type N-terminal domain and an Amy3D-type barrel structure , inherited enzymatic characteristics from the both isozymes .
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Score: 4.00
Title: Characterization of rice alpha-amylase isozymes expressed by Saccharomyces cerevisiae .
Author: Terashima M Katoh S Thomas BR Rodriguez RL .
Journal: Appl . Microbiol . Biotechnol . Citation: V : 43 ( 6 ) P : 1050-5 Year: 1995 Type: ARTICLE
Literature: oryza Field: abstract Doc ID: pub8590656 Accession (PMID): 8590656
Abstract: Two rice alpha-amylase isozymes , AmylA and Amy3D , were produced by secretion from genetically engineered strains of Saccharomyces cerevisiae . They have distinct differences in enzymatic characteristics that can be related to the physiology of the germinating rice seed . The rice isozymes were purified with immunoaffinity chromatography . The pH optima for Amy3D ( pH optimum 5 . 5 ) and Amy1A ( pH optimum 4 . 2 ) correlate with the pH of the endosperm it issue at the times in rice seedling development when these isozymes are produced . Amy3D showed 10-14 times higher reactivity to oligosaccharides than Amy1A . Amy1A , on the other hand , showed higher reactivity to soluble starch and starch granules than Amy3D . These results suggest that the isozyme Amy3D , which is expressed at an early stage of germination , produces sugars from soluble starch during the early stage of seed germination and that the isozyme Amy1A works to initiate hydrolysis of the starch granules .
Matching Sentences:
[ Sen. 4, subscore: 1.00 ]: The pH optima for Amy3D ( pH optimum 5 . 5 ) and Amy1A ( pH optimum 4 . 2 ) correlate with the pH of the endosperm it issue at the times in rice seedling development when these isozymes are produced .
[ Sen. 5, subscore: 1.00 ]: Amy3D showed 10-14 times higher reactivity to oligosaccharides than Amy1A .
[ Sen. 6, subscore: 1.00 ]: Amy1A , on the other hand , showed higher reactivity to soluble starch and starch granules than Amy3D .
[ Sen. 7, subscore: 1.00 ]: These results suggest that the isozyme Amy3D , which is expressed at an early stage of germination , produces sugars from soluble starch during the early stage of seed germination and that the isozyme Amy1A works to initiate hydrolysis of the starch granules .
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Score: 3.00
Title: The roles of the N-linked carbohydrate chain of rice alpha-amylase in thermostability and enzyme kinetics .
Author: Terashima M Kubo A Suzawa M Itoh Y Katoh S
Journal: Eur . J Biochem . Citation: V : 226 ( 1 ) P : 249-54 Year: 1994 Type: ARTICLE
Literature: oryza Field: abstract Doc ID: pub7957256 Accession (PMID): 7957256
Abstract: The thermostability and kinetics of starch hydrolysis were compared between a rice alpha-amylase isozyme Amy1A and its mutant enzyme that lacks an N-linked carbohydrate chain . Elimination of the N-glycosylation site in Amy1A reduced the thermostability of the enzyme . The temperature dependence of the kinetic parameters ( Vm and Km ) and substrate recognition of the enzymes were also affected by elimination of the N-glycosylation site . These results suggest that the N-linked carbohydrate chain of Amy1A has important roles in the thermostability and reaction kinetics of the enzyme .
Matching Sentences:
[ Sen. 1, subscore: 1.00 ]: The thermostability and kinetics of starch hydrolysis were compared between a rice alpha-amylase isozyme Amy1A and its mutant enzyme that lacks an N-linked carbohydrate chain .
[ Sen. 2, subscore: 1.00 ]: Elimination of the N-glycosylation site in Amy1A reduced the thermostability of the enzyme .
[ Sen. 4, subscore: 1.00 ]: These results suggest that the N-linked carbohydrate chain of Amy1A has important roles in the thermostability and reaction kinetics of the enzyme .
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Score: 1.00
Title: Differential expression of rice alpha-amylase genes during seedling development under anoxia .
Author: Hwang YS Thomas BR Rodriguez RL .
Journal: Plant Mol . Biol . Citation: V : 40 ( 6 ) P : 911-20 Year: 1999 Type: ARTICLE
Literature: oryza Field: abstract Doc ID: pub10527416 Accession (PMID): 10527416
Abstract: The unique capability of rice ( Oryza sativa L ) seedlings to grow under anoxic conditions may result in part from their ability to express alpha-amylase and maintain the supply of sugar needed for energy metabolism . Previous studies have demonstrated that under aerobic conditions the Amy1 and Amy2 subfamily genes are regulated primarily by phytohormones while the Amy3 subfamily genes are induced during sugar starvation . The expression patterns for these alpha-amylase genes were considerably different in anoxic vs aerobic rice seedlings . The level of total alpha-amylase mRNA under anoxic conditions was decreased in aleurone layers while it increased in the embryo . Anoxic conditions greatly diminished the expression of the Amy1A gene in aleurone . Conversely , expression of many Amy3 subfamily genes was up-regulated and prolonged in embryo it issues under anoxic conditions .
Matching Sentences:
[ Sen. 5, subscore: 1.00 ]: Anoxic conditions greatly diminished the expression of the Amy1A gene in aleurone .
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