限界デキストリナーゼ
- 関
- pullulanase
WordNet
- restrict or confine, "I limit you to two visits to the pub a day" (同)circumscribe, confine
- the mathematical value toward which a function goes as the independent variable approaches infinity (同)limit_point, point of accumulation
- the greatest amount of something that is possible or allowed; "there are limits on the amount you can bet"; "it is growing rapidly with no limitation in sight" (同)limitation
- the greatest possible degree of something; "what he did was beyond the bounds of acceptable behavior"; "to the limit of his ability" (同)bound, boundary
- the boundary of a specific area (同)demarcation, demarcation line
- as far as something can go
- small in range or scope; "limited war"; "a limited success"; "a limited circle of friends"
- mediocre (同)modified
- having a specific function or scope; "a special (or specific) role in the mission" (同)special
- including only a part
- not excessive
- not unlimited; "a limited list of choices"
- strictly limiting the reference of a modified word or phrase; "the restrictive clause in `Each made a list of the books that had influenced him limits the books on the list to only those particular ones defined by the clause"
PrepTutorEJDIC
- (空間・行為などの)『限界』,《+『of』+『名』》 / 《しばしば複数形で;単数扱い》『境界』,境界線範囲,区域 / (数量などの)許容量,制限 / 適度に / …‘を'『制限する』
- 限られた,狭い / 《米》(鉄道・バスなどが)特別の,特急の / 《英》(会社が)有限の(《米》incorporated) / 特急列車(バスなど)
- 制限する,限定する
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2017/03/07 19:22:52」(JST)
[Wiki en表示]
| Limit dextrinase |
| Identifiers |
| EC number |
3.2.1.142 |
| Databases |
| IntEnz |
IntEnz view |
| BRENDA |
BRENDA entry |
| ExPASy |
NiceZyme view |
| KEGG |
KEGG entry |
| MetaCyc |
metabolic pathway |
| PRIAM |
profile |
| PDB structures |
RCSB PDB PDBe PDBsum |
| Search |
| PMC |
articles |
| PubMed |
articles |
| NCBI |
proteins |
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Limit dextrinase (EC 3.2.1.142, R-enzyme, amylopectin-1,6-glucosidase, dextrin alpha-1,6-glucanohydrolase) is an enzyme with systematic name dextrin 6-alpha-glucanohydrolase.[1][2] This enzyme catalyses the Hydrolysis of (1->6)-alpha-D-glucosidic linkages in alpha- and beta-limits dextrins of amylopectin and glycogen,in amylopectin and pullulan.
References
- ^ Gordon, R.W.; Manners, D.J.; Stark, J.R. (1975). "The limit dextrinase of the broad bean (Vicia faba)". Carbohydr. Res. 42: 125–134. doi:10.1016/s0008-6215(00)84105-1.
- ^ Manners, D.J. (1997). "Observations on the specificity and nomenclature of starch debranching enzymes". J. Appl. Glycosci. 44: 83–85.
See also
- Sucrase-isomaltase, an enzyme
- Pullulanase, an enzyme
External links
- Limit dextrinase at the US National Library of Medicine Medical Subject Headings (MeSH)
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Hydrolase: sugar hydrolases (EC 3.2)
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| 3.2.1: Glycoside hydrolases |
| Disaccharidase |
- Sucrase/Sucrase-isomaltase/Invertase
- Maltase
- Trehalase
- Lactase
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| Glucosidases |
- Cellulase
- Alpha-glucosidase
- Acid
- Neutral AB
- Neutral C
- Beta-glucosidase
- Debranching enzyme
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| Other |
- Amylase
- Chitinase
- Lysozyme
- Neuraminidase
- NEU1
- NEU2
- NEU3
- NEU4
- Bacterial neuraminidase
- Viral neuraminidase
- Galactosidases
- alpha-Mannosidase
- Glucuronidase
- Hyaluronidase
- Pullulanase
- Glucosylceramidase
- Galactosylceramidase
- Alpha-N-acetylgalactosaminidase
- Alpha-N-acetylglucosaminidase
- Fucosidase
- Hexosaminidase
- Iduronidase
- Maltase-glucoamylase
- Heparanase
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3.2.2: Hydrolysing
N-Glycosyl compounds |
- DNA glycosylases: Oxoguanine glycosylase
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Enzymes
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| Activity |
- Active site
- Binding site
- Catalytic triad
- Oxyanion hole
- Enzyme promiscuity
- Catalytically perfect enzyme
- Coenzyme
- Cofactor
- Enzyme catalysis
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| Regulation |
- Allosteric regulation
- Cooperativity
- Enzyme inhibitor
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| Classification |
- EC number
- Enzyme superfamily
- Enzyme family
- List of enzymes
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| Kinetics |
- Enzyme kinetics
- Eadie–Hofstee diagram
- Hanes–Woolf plot
- Lineweaver–Burk plot
- Michaelis–Menten kinetics
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| Types |
- EC1 Oxidoreductases (list)
- EC2 Transferases (list)
- EC3 Hydrolases (list)
- EC4 Lyases (list)
- EC5 Isomerases (list)
- EC6 Ligases (list)
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UpToDate Contents
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English Journal
- Synthesis and physico-chemical characterization of modified starches from banana (Musa AAB) and its biological activities in diabetic rats.
- Reddy CK1, Suriya M2, Vidya PV2, Haripriya S3.
- International journal of biological macromolecules.Int J Biol Macromol.2017 Jan;94(Pt A):500-507. doi: 10.1016/j.ijbiomac.2016.10.050. Epub 2016 Oct 18.
- This study describes a simple method of preparation and physico-chemical properties of modified starches (type-3 resistant starches) from banana (Musa AAB), and the modified starches investigated as functional food with a beneficial effect on type-2 diabetes. RS3 was prepared using a method combined
- PMID 27769930
- Domestication and the storage starch biosynthesis pathway: signatures of selection from a whole sorghum genome sequencing strategy.
- Campbell BC1, Gilding EK1, Mace ES2, Tai S3, Tao Y4, Prentis PJ5, Thomelin P6, Jordan DR4, Godwin ID1.
- Plant biotechnology journal.Plant Biotechnol J.2016 Dec;14(12):2240-2253. doi: 10.1111/pbi.12578. Epub 2016 Jun 11.
- Next-generation sequencing of complete genomes has given researchers unprecedented levels of information to study the multifaceted evolutionary changes that have shaped elite plant germplasm. In conjunction with population genetic analytical techniques and detailed online databases, we can more accu
- PMID 27155090
- Expression and biochemical characterization of a novel type I pullulanase from Bacillus megaterium.
- Yang S1, Yan Q2, Bao Q2, Liu J1, Jiang Z3.
- Biotechnology letters.Biotechnol Lett.2016 Nov 17. [Epub ahead of print]
- OBJECTIVES: To identify novel pullulanases from microorganisms and to investigate their biochemical characterizations.RESULTS: A novel pullulanase gene (BmPul) from Bacillus megaterium WW1210 was cloned and heterologously expressed in Escherichia coli. The gene has an ORF of 2814 bp encoding 937 ami
- PMID 27858318
Japanese Journal
- Surface Binding Sites (SBSs), Mechanism and Regulation of Enzymes Degrading Amylopectin and α-Limit Dextrins
- MOLLER Marie S.,COCKBURN Darrell,NIELSEN Jonas W.,JENSEN Johanne M.,VESTER-CHRISTENSEN Malene B.,NIELSEN Morten M.,ANDERSEN Joakim M.,WILKENS Casper,RANNES Julie,HAGGLUND Per,HENRIKSEN Anette,HACHEM Maher Abou,WILLEMOES Martin,SVENSSON Birte
- Journal of applied glycoscience 60(2), 101-109, 2013-05-20
- NAID 10031159341
- Surface Binding Sites (SBSs), Mechanism and Regulation of Enzymes Degrading Amylopectin and α-Limit Dextrins
- Moller Marie S.,Cockburn Darrell,Nielsen Jonas W. [他]
- Journal of applied glycoscience 60(2), 101-109, 2013
- NAID 40019649183
- Surface Binding Sites (SBSs), Mechanism and Regulation of Enzymes Degrading Amylopectin and α-Limit Dextrins
- , , , , , , , , , , , , ,
- Journal of Applied Glycoscience 60(2), 101-109, 2013
- … New insight into barley seed α-amylase 1 (AMY1) and limit dextrinase (LD) includes i) kinetics of bi-exponential amylopectin hydrolysis by AMY1, one reaction having low Km (8 µg/mL) and high kcat (57 s－1) and the other high Km (97 µg/mL) and low kcat (23 s－1). … LD is controlled by barley limit dextrinase inhibitor (LDI) which belongs to the cereal-type inhibitor family and forms a tight 1:1 complex with LD. …
- NAID 130004481028
Related Links
- limit dextrinase n. An enzyme that catalyzes the hydrolysis of polysaccharides, especially completing the digestion of starch or the conversion of glycogen to glucose.
- limit dextrinase /lim·it dex·trin·ase/ (lim´it deks´trin-ās) α. limit dextrinase n. An enzyme that catalyzes the hydrolysis of polysaccharides, especially completing the digestion of starch or the conversion of glycogen to glucose.
★リンクテーブル★
[★]
- 英
- isomaltase
- 同
- 限界デキストリナーゼ limit dextrinase
- 関
- オリゴ-1,6-グルコシダーゼ
[★]
- 英
- limit dextrinase
- 関
- プルラナーゼ
[★]
プルラナーゼ
- 関
- limit dextrinase
[★]
- 関
- circumscription、confine、confinement、define、definite、definition、extent、limitation、margin、qualify、restrain、restraint、restrict、restriction
[★]
- 関
- rate-determining、rate-limiting、utmost
[★]
- 関
- finite