α-amylase from Mon Thong durian (Durio zibethinus Murr. cv. Mon Thong) : nucleotide sequence analysis, cloning and expression
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DOI[10.5511/plantbiotechnology.14.1122a]to the data of the same series
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- Material Type
- 記事
- Author/Editor
- Saijai PosoongnoenRaksmont UbonbalSompong Thammasirirak
- Publication, Distribution, etc.
- Publication Date
- 2015
- Publication Date (W3CDTF)
- 2015
- Periodical title
- Plant biotechnology
- No. or year of volume/issue
- 32(1)
- Volume
- 32(1)
- ISSN (Periodical Title)
- 1347-6114
- ISSN-L (Periodical Title)
- 1342-4580
- Text Language Code
- eng
- DOI
- 10.5511/plantbiotechnology.14.1122a
- Persistent ID (NDL)
- info:ndljp/pid/11000412
- Collection
- Collection (Materials For Handicapped People:1)
- Collection (particular)
- 国立国会図書館デジタルコレクション > 電子書籍・電子雑誌 > 学術機関 > 学協会
- Acquisition Basis
- インターネット資料収集保存事業（WARP）
- Date Accepted (W3CDTF)
- 2017-12-08T10:56:38+09:00
- Date Captured (W3CDTF)
- 2015-08-15
- Format (IMT)
- application/pdf
- Access Restrictions
- インターネット公開
- Availability of remote photoduplication service
- 不可
- Periodical Title (URI)
- Periodical Title (Persistent ID (NDL))
- info:ndljp/pid/11000411
- Data Provider (Database)
- 国立国会図書館 : 国立国会図書館デジタルコレクション
- Collection (particular)
- 国立国会図書館デジタルコレクション > 電子書籍・電子雑誌 > 学術機関 > 学協会
- Access Restrictions
- インターネット公開
- Availability of remote photoduplication service
- 不可
- Holding library
- 国立国会図書館
- Call No.
- Z54-J126
- Related Material (URI)
- Related Material (Persistent ID (NDL))
- info:ndljp/pid/11000412
- Data Provider (Database)
- 国立国会図書館 : 国立国会図書館雑誌記事索引
- Bibliographic ID (NDL)
- 026292476
- Bibliographic Record Category (NDL)
- 632
- Summary, etc.
- Amylase is hypothesized to involve in the initiation of intracellular starch granule digestion in the plastids of ripening durians. A putative α-amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong; DzAmy3) was successfully isolated and its gene contain a 2,679 base pair open reading frame, which encodes 892 amino acids with a calculated molecular mass of 93.7 kDa and an isoelectric point of 5.77. The DzAmy3 contains starch binding domain with a putative plastid transit peptide and α-amylase like domain. Phylogenetic tree analysis proved it into the family three of plant α-amylases. The predicted structural model proposed a catalytic triad (Asp611, Glu636 and Asp719) for general acid/base hydrolysis. Recombinant DzAmy3 (rDzAmy3) was successfully expressed in <i>Escherichia coli</i>. rDzAmy3 hydrolyzed starch and ethylidene-pNP-G7 which confirms the authenticity of DzAmy3 gene and functional α-amylase. The rDzAmy3 had an optimum activity at pH 8.0 and 30°C. It was stable in the pH range of 7–8 at 37°C, temperature range of 5–20°C and in the presence of 1% (v/v) Tween 20 and Triton X-100. Substrate specificity analysis revealed that rDzAmy3 was active toward β-limit dextrin, starch, amylopectin, amylose and glycogen.
- DOI
- 10.5511/plantbiotechnology.14.1122a
- Access Restrictions
- インターネット公開
- Data Provider (Database)
- 科学技術振興機構 : J-STAGE
- Summary, etc.
- Amylase is hypothesized to involve in the initiation of intracellular starch granule digestion in the plastids of ripening durians. A putative α-amylase from Mon Thong durian (<i>Durio zibethinus</i> Murr. cv. Mon Thong; DzAmy3) was successfully isolated and its gene contain a 2,679 base pair open reading frame, which encodes 892 amino acids with a calculated molecular mass of 93.7 kDa and an isoelectric point of 5.77. The DzAmy3 contains starch binding domain with a putative plastid transit peptide and α-amylase like domain. Phylogenetic tree analysis proved it into the family three of plant α-amylases. The predicted structural model proposed a catalytic triad (Asp611, Glu636 and Asp719) for general acid/base hydrolysis. Recombinant DzAmy3 (rDzAmy3) was successfully expressed in <i>Escherichia coli</i>. rDzAmy3 hydrolyzed starch and ethylidene-pNP-G7 which confirms the authenticity of DzAmy3 gene and functional α-amylase. The rDzAmy3 had an optimum activity at pH 8.0 and 30°C. It was stable in the pH range of 7–8 at 37°C, temperature range of 5–20°C and in the presence of 1% (v/v) Tween 20 and Triton X-100. Substrate specificity analysis revealed that rDzAmy3 was active toward β-limit dextrin, starch, amylopectin, amylose and glycogen.
- DOI
- 10.5511/plantbiotechnology.14.1122a
- Access Restrictions
- インターネット公開
- Related Material (URI)
- Is Referenced By
- Purification and characterization of thermostable α-amylase from germinating Sword bean (Canavalia gladiata (Jacq.) DC.) seeds
- References
- Crystal and Molecular Structure of Barley α-AmylaseProperties and applications of starch-converting enzymes of the α-amylase familyBarley α‐amylase Met53 situated at the high‐affinity subsite −2 belongs to a substrate binding motif in the β→α loop 2 of the catalytic (β/α)<sub>8</sub>‐barrel and is critical for activity and substrate specificityα-Amylase from germinating soybean (Glycine max) seeds – Purification, characterization and sequential similarity of conserved and catalytic amino acid residuesChloroP, a neural network‐based method for predicting chloroplast transit peptides and their cleavage sitesα-Amylase from mung beans (Vigna radiata) – Correlation of biochemical properties and tertiary structure by homology modellingCloning, Expression, Purification, and Characterization of Cold-Adapted α-Amylase from Pseudoalteromonas arctica GS230Starch‐binding domains in the CBM45 family – low‐affinity domains from glucan, water dikinase and α‐amylase involved in plastidial starch metabolismClustal W and Clustal X version 2.0InterPro: the integrative protein signature databaseReview: cyclodextrins and their interaction with amylolytic enzymesThe Carbohydrate-Active EnZymes database (CAZy): an expert resource for GlycogenomicsA study of the effect of the drying process on the composition and physicochemical properties of flours obtained from durian fruits of two ripening stagesOligosaccharide Binding to Barley α-Amylase 1Purification and characterization of α-amylase from safflower (Carthamus tinctorius L.) germinating seedsExploring the potential nutraceutical values of durian (Durio zibethinus L.) – An exotic tropical fruitSite-directed mutagenesis of histidine 93, aspartic acid 180, glutamic acid 205, histidine 290, and aspartic acid 291 at the active site and tryptophan 279 at the raw starch binding site in barley alpha-amylase 1.Application of microbial α-amylase in industry - A reviewA Novel Type Carbohydrate-Binding Module Identified in α-Glucan, Water Dikinases Is Specific for Regulated Plastidial Starch MetabolismMolecular Cloning and Expression of α-Globin and β-Globin Genes from Crocodile (Crocodylus siamensis)Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugarα-Amylase Is Not Required for Breakdown of Transitory Starch in Arabidopsis LeavesChromatographic methods for amylasesSWISS-MODEL: an automated protein homology-modeling serverBiochemistry of Fruit RipeningCDD: a conserved domain database for interactive domain family analysisMEGA5: Molecular Evolutionary Genetics Analysis Using Maximum Likelihood, Evolutionary Distance, and Maximum Parsimony MethodsPurification and some properties of α-amylase from post-harvest Pachyrhizus erosus L. tuberMango Starch Degradation. II. The Binding of α-Amylase and β-Amylase to the Starch GranuleThe SWISS-MODEL Repository and associated resourcesMolecular structure of a barley α-amylase-inhibitor complex: implications for starch binding and catalysisIdentification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sitesPhysiological changes during postharvest ripening of durian fruit (<i>Durio zibethinus</i>Murray)Predicting Subcellular Localization of Proteins Based on their N-terminal Amino Acid SequenceThe ‘pair of sugar tongs’ site on the non‐catalytic domain C of barley α‐amylase participates in substrate binding and activityThe SWISS-MODEL workspace: a web-based environment for protein structure homology modellingAn E. coli Expression System for the Extracellular Secretion of Barley α-AmylaseArabidopsis thaliana AMY3 Is a Unique Redox-regulated Chloroplastic α-AmylaseDurianThe Structure of Barley α-Amylase Isozyme 1 Reveals a Novel Role of Domain C in Substrate Recognition and BindingCDD: specific functional annotation with the Conserved Domain Database
- Data Provider (Database)
- 国立情報学研究所 : CiNii Research
- Original Data Provider (Database)
- Japan Link Center雑誌記事索引データベース雑誌記事索引データベースCrossrefCiNii ArticlesCrossref
- Bibliographic ID (NDL)
- 02629247611000412
- NAID
- 130005061607