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CATH domain | Related DB codes (homologues) |
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2.60.40.10 : Immunoglobulin-like | M00131,T00257,T00005,M00113,M00127,M00132,M00323,M00325,M00327,M00329,M00330,M00331,M00332,T00307,D00166,D00500,M00112,M00193,T00063,T00065,T00245 | 2.60.40.1180 : Immunoglobulin-like | M00113,T00307,D00165,D00176,D00664,D00665,D00863,D00864,M00112,M00193,M00314,T00057,T00062 | 3.20.20.80 : TIM Barrel | S00202,S00210,S00748,S00906,S00907,S00911,S00912,S00915,M00134,M00160,D00479,S00204,S00205,S00206,S00207,S00203,S00208,S00209,S00211,S00213,S00214,M00113,T00307,D00165,D00166,D00169,D00176,D00501,D00502,D00503,D00844,D00861,D00864,M00026,M00112,M00193,M00346,T00057,T00062,T00063,T00066 |
UniProtKB:Accession Number | P10342 |
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Entry name | ISOA_PSEAY |
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Activity | Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins. |
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Subunit | Monomer. |
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Subcellular location |
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Cofactor | Binds 1 calcium ion per subunit. |
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References for Catalytic Mechanism | References | Sections | No. of steps in catalysis |
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[3] | p.890-892 |
| [4] | Fig.2, p.4-5, p.11 |
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references | [1] |
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PubMed ID | 7175943 |
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Journal | J Mol Biol |
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Year | 1982 |
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Volume | 160 |
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Pages | 669-71 |
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Authors | Sato M, Hato Y, Ii Y, Miki K, Kasai N, Tanaka N, Harada T |
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Title | Preliminary x-ray studies on Pseudomonas isoamylase. |
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[2] |
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PubMed ID | 1388153 |
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Journal | J Biol Chem |
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Year | 1992 |
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Volume | 267 |
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Pages | 18447-52 |
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Authors | Takata H, Kuriki T, Okada S, Takesada Y, Iizuka M, Minamiura N, Imanaka T |
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Title | Action of neopullulanase. Neopullulanase catalyzes both hydrolysis and transglycosylation at alpha-(1----4)- and alpha-(1----6)-glucosidic linkages. |
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[3] |
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Comments | X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). |
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Medline ID | 98387895 |
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PubMed ID | 9719642 |
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Journal | J Mol Biol |
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Year | 1998 |
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Volume | 281 |
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Pages | 885-97 |
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Authors | Katsuya Y, Mezaki Y, Kubota M, Matsuura Y |
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Title | Three-dimensional structure of Pseudomonas isoamylase at 2.2 A resolution. |
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Related PDB | 1bf2 |
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Related UniProtKB | P10342 |
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[4] |
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PubMed ID | 11257505 |
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Journal | Biochim Biophys Acta |
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Year | 2001 |
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Volume | 1546 |
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Pages | 1-20 |
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Authors | MacGregor EA, Janecek S, Svensson B |
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Title | Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. |
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[5] |
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PubMed ID | 12509527 |
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Journal | Plant Cell |
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Year | 2003 |
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Volume | 15 |
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Pages | 133-49 |
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Authors | Hussain H, Mant A, Seale R, Zeeman S, Hinchliffe E, Edwards A, Hylton C, Bornemann S, Smith AM, Martin C, Bustos R |
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Title | Three isoforms of isoamylase contribute different catalytic properties for the debranching of potato glucans. |
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comments | This enzyme belongs to the glycosyl hydrolase family-13. Although this enzyme binds a calcium ion, it is not involved in catalysis. The literature [4] suggests that this enzyme must have a similar catalytic mechanism to that of alpha-amylase (D00165 in EzCatDB). It catalyzes the hydrolysis of (1->6)-alpha-D-glucosidic linkage. Asp375 acts as a nucleophile, whilst Glu435 acts as general acid-base.
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created | updated |
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2005-03-31 | 2009-02-26 |
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