Glycogen debranching enzyme: Difference between revisions

Revision as of 22:13, 31 October 2018

Revision as of 16:21, 16 February 2019

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[[File:Hypothesized substraight binding ___location.png]]

The structure of the ''Candida glabrata'' GDE has been reported.<ref>{{Cite journal|last=Zhai|first=Liting|last2=Feng|first2=Lingling|last3=Xia|first3=Lin|last4=Yin|first4=Huiyong|last5=Xiang|first5=Song|date=2016-04-18|title=Crystal structure of glycogen debranching enzyme and insights into its catalysis and disease-causing mutations|url=https://www.nature.com/articles/ncomms11229|journal=Nature Communications|language=en|volume=7|pages=ncomms11229|doi=10.1038/ncomms11229|pmid=27088557|pmc=4837477}}</ref> The structure revealed that distinct domains in GDE encode the glucanotransferase and glucosidase activities. Their catalyses are similar to that of alpha-amylase and glucoamylase, respectively. Their active sites are selective towards the respective substrates, ensuring proper activation of GDE. Besides the active sites GDE have additional binding sites for glycogen, which are important for its recruitment to glycogen. Mapping the disease-causing mutations onto the GDE structure provided insights into glycogen storage disease type III.

== Genetic ___location ==

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<ref name="Bao">{{cite journal |vauthors=Bao Y, Dawson TL, Chen YT | title = Human glycogen debranching enzyme gene (AGL): complete structural organization and characterization of the 5' flanking region | journal = Genomics | volume = 38 | issue = 2 | pages = 155–65 |date=December 1996 | pmid = 8954797 | doi = 10.1006/geno.1996.0611}}</ref>

<ref name="Berg">{{cite book | last1 = Stryer | first1 = Lubert | last2 = Berg | first2 = Jeremy Mark | last3 = Tymoczko | first3 = John L. | name-list-format = vanc | title = Biochemistry | edition = 6th | language = | publisher = W.H. Freeman | ___location = San Francisco | year = 2007 | origyear = | pages = | quote = | isbn = 978-0-7167-8724-52 | oclc = | doi = | url = | accessdate = }}</ref>

<ref name="Dauvillée">{{cite journal |vauthors=Dauvillée D, Kinderf IS, Li Z, Kosar-Hashemi B, Samuel MS, Rampling L, Ball S, Morell MK | title = Role of the Escherichia coli glgX gene in glycogen metabolism | journal = J. Bacteriol. | volume = 187 | issue = 4 | pages = 1465–73 |date=February 2005 | pmid = 15687211 | pmc = 545640 | doi = 10.1128/JB.187.4.1465-1473.2005 }}</ref>

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<ref name="Chen">{{cite journal |vauthors=Chen YT, He JK, Ding JH, Brown BI | title = Glycogen debranching enzyme: purification, antibody characterization, and immunoblot analyses of type III glycogen storage disease | journal = Am. J. Hum. Genet. | volume = 41 | issue = 6 | pages = 1002–15 |date=December 1987 | pmid = 2961257 | pmc = 1684360 | doi = }}</ref>

<ref name="UniProt P35573">{{cite web | url = https://www.uniprot.org/uniprot/P35573 | title = Glycogen debranching enzyme - Homo sapiens (Human) | date = | format = | workwebsite = | publisher = UniProt | pages = | language = | archiveurl = | archivedate = | quote = | accessdate = }}</ref>

<ref name="Gillard_80">{{cite journal |vauthors=Gillard BK, White RC, Zingaro RA, Nelson TE | title = Amylo-1,6-glucosidase/4-alpha-glucanotransferase. Reaction of rabbit muscle debranching enzyme with an active site-directed irreversible inhibitor, 1-S-dimethylarsino-1-thio-beta-D-glucopyranoside | journal = J. Biol. Chem. | volume = 255 | issue = 18 | pages = 8451–7 |date=September 1980 | pmid = 6447697 | doi = }}</ref>

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<ref name="Woo">{{cite journal |vauthors=Woo EJ, Lee S, Cha H, Park JT, Yoon SM, Song HN, Park KH | title = Structural insight into the bifunctional mechanism of the glycogen-debranching enzyme TreX from the archaeon Sulfolobus solfataricus | journal = J. Biol. Chem. | volume = 283 | issue = 42 | pages = 28641–8 |date=October 2008 | pmid = 18703518 | pmc = 2661413 | doi = 10.1074/jbc.M802560200 }}</ref>

<ref name="UniProt A8QX06">{{cite web | url = https://www.uniprot.org/uniprot/A8QX06 | title = TreX - Actinoplanes sp. SN223/29 | date = | format = | workwebsite = | publisher = UniProt | pages = | language = | archiveurl = | archivedate = | quote = | accessdate = }}</ref>

<ref name="UniProt A7ZSW4">{{cite web | url = https://www.uniprot.org/uniprot/A7ZSW4 | title = Glycogen debranching enzyme - Escherichia coli O139:H28 (strain E24377A / ETEC) | date = | format = | workwebsite = | publisher = UniProt | pages = | language = | archiveurl = | archivedate = | quote = | accessdate = }}</ref>

<ref name="UniProt P15977">{{cite web | url = https://www.uniprot.org/uniprot/P15977 | title = 4-alpha-glucanotransferase - Escherichia coli (strain K12) | date = | format = | workwebsite = | publisher = | pages = | language = | archiveurl = | archivedate = | quote = | accessdate = }}</ref>

<ref name="Park">{{cite journal |vauthors=Park JT, Park HS, Kang HK, Hong JS, Cha H, Woo EJ, Kim JW, Kim MJ, Boos W, Lee S, Park KH | title = Oligomeric and functional properties of a debranching enzyme (TreX) from the archaeon Sulfobus solfataricus P2. | journal = Biocatalysis and Biotransformation | year = 2008 | volume = 26 | issue = 1–2 | pages = 76–85 | doi = 10.1080/10242420701806652 }}</ref>

<ref name="Talente">{{cite journal |vauthors=Talente GM, Coleman RA, Alter C, Baker L, Brown BI, Cannon RA, Chen YT, Crigler JF, Ferreira P, Haworth JC, Herman GE, Issenman RM, Keating JP, Linde R, Roe TF, Senior B, Wolfsdorf JI | display-authors = 6 | title = Glycogen storage disease in adults | journal = Ann. Intern. Med. | volume = 120 | issue = 3 | pages = 218–26 |date=February 1994 | pmid = 8273986 | doi = 10.7326/0003-4819-120-3-199402010-00008}}</ref>

<ref name="Monga">{{cite book | first = Satdarshan P. S. | last = Monga | name-list-format = vanc | title = Molecular Pathology of Liver Diseases (Molecular Pathology Library) | publisher = Springer | ___location = Berlin | year = 2010 | pages = | isbn = 978-1-4419-7106-87 }}</ref>

<ref name="Hondoh">{{cite journal |vauthors=Hondoh H, Saburi W, Mori H, etal | title = Substrate recognition mechanism of alpha-1,6-glucosidic linkage hydrolyzing enzyme, dextran glucosidase from Streptococcus mutans | journal = J. Mol. Biol. | volume = 378 | issue = 4 | pages = 913–22 |date=May 2008 | pmid = 18395742 | doi = 10.1016/j.jmb.2008.03.016 }}</ref>