DB code: T00067
| RLCP classification | 1.30.36000.3 : Hydrolysis | |
|---|---|---|
| CATH domain | 2.60.40.10 : Immunoglobulin-like | |
| 3.20.20.80 : TIM Barrel | Catalytic domain | |
| 2.60.40.1180 : Immunoglobulin-like | ||
| E.C. | 3.2.1.68 | |
| CSA | 1bf2 | |
| M-CSA | 1bf2 | |
| MACiE | ||
| CATH domain | Related DB codes (homologues) |
|---|---|
| 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 |
| Uniprot Enzyme Name | UniprotKB | Protein name | Synonyms | CAZy | Pfam |
|---|---|---|---|---|
| P10342 |
Isoamylase
|
EC
3.2.1.68
|
CBM48
(Carbohydrate-Binding Module Family 48)
GH13 (Glycoside Hydrolase Family 13) |
PF00128
(Alpha-amylase)
PF02922 (CBM_48) [Graphical View] |
| KEGG enzyme name |
|---|
|
isoamylase
debranching enzyme glycogen alpha-1,6-glucanohydrolase |
| UniprotKB: Accession Number | Entry name | Activity | Subunit | Subcellular location | Cofactor |
|---|---|---|---|---|---|
| P10342 | ISOA_PSEAY | Hydrolysis of (1->6)-alpha-D-glucosidic branch linkages in glycogen, amylopectin and their beta-limit dextrins. | Monomer. | Binds 1 calcium ion per subunit. |
| KEGG Pathways | Map code | Pathways | E.C. |
|---|
| Compound table | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Substrates | Products | Intermediates | |||||||||
| KEGG-id | C00182 | C00317 | C00001 | C00718 | C00721 | ||||||
| E.C. | |||||||||||
| Compound | Glycogen | Amylopectin | H2O | Amylose | Dextrin | ||||||
| Type | polysaccharide | polysaccharide | H2O | polysaccharide | polysaccharide | ||||||
| ChEBI |
28087 28087 |
28057 28057 |
15377 15377 |
||||||||
| PubChem |
439177 439177 |
439207 439207 |
22247451 962 22247451 962 |
||||||||
| 1bf2A01 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1bf2A02 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| 1bf2A03 |
|
|
|
|
|
Unbound | Unbound | Unbound | Unbound | ||
| Reference for Active-site residues | ||
|---|---|---|
| resource | references | E.C. |
| Swiss-prot;P10342 & literature [3] | ||
| Active-site residues | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|
| PDB | Catalytic residues | Cofactor-binding residues | Modified residues | Main-chain involved in catalysis | Comment | |||||
| 1bf2A01 |
|
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|
|
|
|||||
| 1bf2A02 |
|
|
|
|
|
ASP 375;GLU 435;ASP 510 | ||||
| 1bf2A03 |
|
|
|
|
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|||||
| References for Catalytic Mechanism | ||
|---|---|---|
| References | Sections | No. of steps in catalysis |
|
[3]
|
p.890-892 | |
|
[4]
|
Fig.2, p.4-5, p.11 | |
| References | |
|---|---|
| [1] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 7175943 |
| Journal | J Mol Biol |
| Year | 1982 |
| Volume | 160 |
| Pages | 669-71 |
| Authors | Sato M, Hato Y, Ii Y, Miki K, Kasai N, Tanaka N, Harada T |
| Title | Preliminary x-ray studies on Pseudomonas isoamylase. |
| Related PDB | |
| Related UniProtKB | |
| [2] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 1388153 |
| Journal | J Biol Chem |
| Year | 1992 |
| Volume | 267 |
| Pages | 18447-52 |
| Authors | Takata H, Kuriki T, Okada S, Takesada Y, Iizuka M, Minamiura N, Imanaka T |
| Title |
Action of neopullulanase. |
| Related PDB | |
| Related UniProtKB | |
| [3] | |
| Resource | |
| Comments | X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). |
| Medline ID | 98387895 |
| PubMed ID | 9719642 |
| Journal | J Mol Biol |
| Year | 1998 |
| Volume | 281 |
| Pages | 885-97 |
| Authors | Katsuya Y, Mezaki Y, Kubota M, Matsuura Y |
| Title | Three-dimensional structure of Pseudomonas isoamylase at 2.2 A resolution. |
| Related PDB | 1bf2 |
| Related UniProtKB | P10342 |
| [4] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 11257505 |
| Journal | Biochim Biophys Acta |
| Year | 2001 |
| Volume | 1546 |
| Pages | 1-20 |
| Authors | MacGregor EA, Janecek S, Svensson B |
| Title | Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes. |
| Related PDB | |
| Related UniProtKB | |
| [5] | |
| Resource | |
| Comments | |
| Medline ID | |
| PubMed ID | 12509527 |
| Journal | Plant Cell |
| Year | 2003 |
| Volume | 15 |
| Pages | 133-49 |
| Authors | Hussain H, Mant A, Seale R, Zeeman S, Hinchliffe E, Edwards A, Hylton C, Bornemann S, Smith AM, Martin C, Bustos R |
| Title | Three isoforms of isoamylase contribute different catalytic properties for the debranching of potato glucans. |
| Related PDB | |
| Related UniProtKB | |
| Comments |
|---|
|
Although this enzyme binds a calcium ion, The literature [4] suggests that this enzyme must have a similar catalytic mechanism to that of alpha-amylase (D00165 in EzCatDB). Asp375 acts as a nucleophile, This enzyme belongs to the glycosyl hydrolase family-13. |
| Created | Updated |
|---|---|
| 2005-03-31 | 2009-02-26 |