1g1y

<table><tr><td colspan='2'>[[1g1y]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43649 Atcc 43649]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G1Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1G1Y FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene></td></tr>

<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Neopullulanase Neopullulanase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.135 3.2.1.135] </span></td></tr>

[[https://www.uniprot.org/uniprot/NEPU2_THEVU NEPU2_THEVU]] Hydrolyzes pullulan efficiently but only a small amount of starch. Endohydrolysis of 1,4-alpha-glucosidic linkages in pullulan to form panose. Cleaves also (1-6)-alpha-glucosidic linkages to form maltotriose.

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== Publication Abstract from PubMed ==

Crystals of the mutant E354A of Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII) complexed with beta-cyclodextrin were prepared by a soaking method, and the diffraction data were collected at 100 K, using Synchrotron radiation (SPring-8). The crystals belong to an orthorhombic system with the space group P2(1)2(1)2(1) and cell dimensions a = 111.1 A, b = 117.7 A, c = 113.3 A, which is almost isomorphous with crystals of the wild-type TVAII, and the structure was refined to an R-factor = 0.208 (R(free) = 0.252) using 3.0 A resolution data. The refined structure shows that the interactions between Phe286 and two C6 atoms of beta-cyclodextrin at the hydrolyzing site are important for TVAII to recognize cyclodextrins as substrates. This observation from the X-ray structure was supported by kinetic analyses of cyclodextrins using the wild-type TVAII, the mutant F286A and F286L. These studies also suggested that the TVAII-hydrolyzing mechanism for cyclodextrins is slightly different from that for starch.

Studies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structure of the mutant E354A complexed with beta-cyclodextrin, and kinetic analyses on cyclodextrins.,Kondo S, Ohtaki A, Tonozuka T, Sakano Y, Kamitori S J Biochem. 2001 Mar;129(3):423-8. PMID:11226882<ref>PMID:11226882</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Atcc 43649]]

[[Category: Neopullulanase]]

[[Category: Kamitori, S]]

[[Category: Kondo, S]]

[[Category: Ohtaki, A]]

[[Category: Sakano, Y]]

[[Category: Tonozuka, T]]

[[Category: Hydrolase]]