EzCatDB: M00112
Related links:    PDB-formatted query search system Fasta-formatted query search system Fasta-formatted query search system

DB codeM00112
RLCP classification1.30.36000.3 : Hydrolysis
CATH domainDomain 13.20.20.80 : TIM BarrelCatalytic domain
Domain 22.60.40.1180 : Immunoglobulin-like
Domain 32.60.40.10 : Immunoglobulin-like
Domain 42.60.40.10 : Immunoglobulin-like
E.C.3.2.1.133
CSA1qho

CATH domainRelated DB codes (homologues)
2.60.40.10 : Immunoglobulin-likeM00131,T00257,T00005,M00113,M00127,M00132,M00323,M00325,M00327,M00329,M00330,M00331,M00332,T00307,D00166,D00500,M00193,T00063,T00065,T00067,T00245
2.60.40.1180 : Immunoglobulin-likeM00113,T00307,D00165,D00176,D00664,D00665,D00863,D00864,M00193,M00314,T00057,T00062,T00067
3.20.20.80 : TIM BarrelS00202,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,M00193,M00346,T00057,T00062,T00063,T00066,T00067

Enzyme Name
UniProtKBKEGG

P19531
Protein nameMaltogenic alpha-amylaseglucan 1,4-alpha-maltohydrolase
maltogenic alpha-amylase
1,4-alpha-D-glucan alpha-maltohydrolase
SynonymsEC 3.2.1.133
Glucan 1,4-alpha-maltohydrolase
PfamPF00128 (Alpha-amylase)
PF02806 (Alpha-amylase_C)
PF00686 (CBM_20)
PF01833 (TIG)
[Graphical view]
CAZyGH13 (Glycoside Hydrolase Family)


UniProtKB:Accession NumberP19531
Entry nameAMYM_BACST
ActivityHydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides so as to remove successive alpha- maltose residues from the non-reducing ends of the chains.
SubunitMonomer.
Subcellular location
CofactorBinds 3 calcium ions per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProductsintermediates
KEGG-idC00076C00369C00721C00001C00897C00369C00721


CompoundCalciumStarchDextrinH2Oalpha-MaltoseStarchDextrinTransition-state in glycosylationGlycosyl-enzyme intermediateTransition-state in deglycosylation
Typedivalent metal (Ca2+, Mg2+)polysaccharidepolysaccharideH2Opolysaccharidepolysaccharidepolysaccharide


ChEBI29108


15377
18167





PubChem271


962
22247451
439341





                  
1qhoA01Bound:3x_CAUnboundUnbound UnboundUnboundUnboundTransition-state-analogue:ABD  
1qhpA01Bound:3x_CAUnboundUnbound Bound:MAL 1290UnboundBound:MAL 1289Unbound  
1qhoA02UnboundUnboundUnbound UnboundUnboundUnboundUnbound  
1qhpA02UnboundUnboundUnbound UnboundUnboundUnboundUnbound  
1qhoA03UnboundUnboundUnbound UnboundUnboundUnboundUnbound  
1qhpA03UnboundUnboundUnbound UnboundUnboundUnboundUnbound  
1qhoA04UnboundUnboundUnbound UnboundUnboundUnboundUnbound  
1qhpA04UnboundUnboundUnbound UnboundUnboundUnboundUnbound  

Active-site residues
pdbCatalytic residuesCofactor-binding residues
          
1qhoA01ASP 228;GLU 256;ASP 329
ASP 21;ASP 23;ASN 26;ASN 27;GLY 48;ASP 50(Calcium-1 binding);ASP 76;ASN 77;ASP 79;GLU 101(Calcium-2 binding);ASN 131;GLN 184;ASP 198;HIS 232(Calcium-3 binding)
1qhpA01ASP 228;GLU 256;ASP 329
ASP 21;ASP 23;ASN 26;ASN 27;GLY 48;ASP 50(Calcium-1 binding);ASP 76;ASN 77;ASP 79;GLU 101(Calcium-2 binding);ASN 131;GLN 184;ASP 198;HIS 232(Calcium-3 binding)
1qhoA02 
 
1qhpA02 
 
1qhoA03 
 
1qhpA03 
 
1qhoA04 
 
1qhpA04 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[4]Fig.4, p.342-343
[6]Fig.4, p.141-143

references
[1]
PubMed ID9401418
JournalProg Biophys Mol Biol
Year1997
Volume67
Pages67-97
AuthorsJanecek S
Titlealpha-Amylase family: molecular biology and evolution.
[2]
PubMed ID10209866
JournalCarbohydr Res
Year1998
Volume313
Pages235-46
AuthorsPark KH, Kim MJ, Lee HS, Han NS, Kim D, Robyt JF
TitleTransglycosylation reactions of Bacillus stearothermophilus maltogenic amylase with acarbose and various acceptors.
[3]
CommentsREVISIONS, AND X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
Medline ID99315215
PubMed ID10387084
JournalBiochemistry
Year1999
Volume38
Pages8385-92
AuthorsDauter Z, Dauter M, Brzozowski AM, Christensen S, Borchert TV, Beier L, Wilson KS, Davies GJ
TitleX-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution.
Related PDB1qho,1qhp
Related UniProtKBP19531
[4]
PubMed ID11150613
JournalBiochim Biophys Acta
Year2000
Volume1543
Pages336-360
Authorsvan der Veen BA, Uitdehaag JC, Dijkstra BW, Dijkhuizen L
TitleEngineering of cyclodextrin glycosyltransferase reaction and product specificity.
[5]
PubMed ID10906346
JournalProtein Eng
Year2000
Volume13
Pages509-13
AuthorsBeier L, Svendsen A, Andersen C, Frandsen TP, Borchert TV, Cherry JR
TitleConversion of the maltogenic alpha-amylase Novamyl into a CGTase.
[6]
PubMed ID11796168
JournalJ Biotechnol
Year2002
Volume94
Pages137-55
Authorsvan der Maarel MJ, van der Veen B, Uitdehaag JC, Leemhuis H, Dijkhuizen L
TitleProperties and applications of starch-converting enzymes of the alpha-amylase family.
[7]
PubMed ID12581203
JournalEur J Biochem
Year2003
Volume270
Pages635-45
AuthorsJanecek S, Svensson B, MacGregor EA
TitleRelation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain.
[8]
PubMed ID12890607
JournalJ Biotechnol
Year2003
Volume103
Pages203-12
AuthorsLeemhuis H, Kragh KM, Dijkstra BW, Dijkhuizen L
TitleEngineering cyclodextrin glycosyltransferase into a starch hydrolase with a high exo-specificity.

comments
This enzyme belongs to the glycosidase family-13.
Although this enzyme binds three calcium ions, they are not involved in catalysis.
Since this enzyme is homologous to alpha-amylase (D00165 in EzCatDB), it must have the same catalytic mechanism as that of the homologue.

createdupdated
2007-01-162009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2012 - March 2013)
Supported by the commission for the Development of Artificial Gene Synthesis Technology for Creating Innovative Biomaterial from the Ministry of Economy, Trade and Industry (METI) (October 2012 - )
© Biotechnology Research Institute for Drug Discovery, AIST, 2015-2016 All Rights Reserved.
© Computational Biology Research Center, AIST, 2004-2016 All Rights Reserved.