DB code: M00112

RLCP classification 1.30.36000.3 : Hydrolysis
CATH domain 3.20.20.80 : TIM Barrel Catalytic domain
2.60.40.1180 : Immunoglobulin-like
2.60.40.10 : Immunoglobulin-like
2.60.40.10 : Immunoglobulin-like
E.C. 3.2.1.133
CSA 1qho
M-CSA 1qho
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 M00193 T00063 T00065 T00067 T00245
2.60.40.1180 : Immunoglobulin-like M00113 T00307 D00165 D00176 D00664 D00665 D00863 D00864 M00193 M00314 T00057 T00062 T00067
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 M00193 M00346 T00057 T00062 T00063 T00066 T00067

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
P19531 Maltogenic alpha-amylase
EC 3.2.1.133
Glucan 1,4-alpha-maltohydrolase
CBM20 (Carbohydrate-Binding Module Family 20)
GH13 (Glycoside Hydrolase Family 13)
PF00128 (Alpha-amylase)
PF02806 (Alpha-amylase_C)
PF00686 (CBM_20)
PF01833 (TIG)
[Graphical View]

KEGG enzyme name
glucan 1,4-alpha-maltohydrolase
maltogenic alpha-amylase
1,4-alpha-D-glucan alpha-maltohydrolase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P19531 AMYM_BACST Hydrolysis 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. Monomer. Binds 3 calcium ions per subunit.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00076 C00369 C00721 C00001 C00897 C00369 C00721
E.C.
Compound Calcium Starch Dextrin H2O alpha-Maltose Starch Dextrin Transition-state in glycosylation Glycosyl-enzyme intermediate Transition-state in deglycosylation
Type divalent metal (Ca2+, Mg2+) polysaccharide polysaccharide H2O polysaccharide polysaccharide polysaccharide
ChEBI 29108
 29108
 		15377
 15377
 		18167
 18167
PubChem 271
 271
 		22247451
 962
 22247451
 962
 		439341
 439341
1qhoA01 Bound:3x_CA Unbound Unbound Unbound Unbound Unbound Transition-state-analogue:ABD
1qhpA01 Bound:3x_CA Unbound Unbound Bound:MAL_1290 Unbound Bound:MAL_1289 Unbound
1qhoA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qhpA02 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qhoA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qhpA03 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qhoA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1qhpA04 Unbound Unbound Unbound Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1qhoA01 ASP 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)
1qhpA01 ASP 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
References Sections No. of steps in catalysis
[4]
Fig.4, p.342-343
[6]
Fig.4, p.141-143

References
[1]
Resource
Comments
Medline ID
PubMed ID 9401418
Journal Prog Biophys Mol Biol
Year 1997
Volume 67
Pages 67-97
Authors Janecek S
Title alpha-Amylase family: molecular biology and evolution.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 10209866
Journal Carbohydr Res
Year 1998
Volume 313
Pages 235-46
Authors Park KH, Kim MJ, Lee HS, Han NS, Kim D, Robyt JF
Title Transglycosylation reactions of Bacillus stearothermophilus maltogenic amylase with acarbose and various acceptors.
Related PDB
Related UniProtKB
[3]
Resource
Comments REVISIONS, AND X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS).
Medline ID 99315215
PubMed ID 10387084
Journal Biochemistry
Year 1999
Volume 38
Pages 8385-92
Authors Dauter Z, Dauter M, Brzozowski AM, Christensen S, Borchert TV, Beier L, Wilson KS, Davies GJ
Title X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution.
Related PDB 1qho 1qhp
Related UniProtKB P19531
[4]
Resource
Comments
Medline ID
PubMed ID 11150613
Journal Biochim Biophys Acta
Year 2000
Volume 1543
Pages 336-360
Authors van der Veen BA, Uitdehaag JC, Dijkstra BW, Dijkhuizen L
Title Engineering of cyclodextrin glycosyltransferase reaction and product specificity.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 10906346
Journal Protein Eng
Year 2000
Volume 13
Pages 509-13
Authors Beier L, Svendsen A, Andersen C, Frandsen TP, Borchert TV, Cherry JR
Title Conversion of the maltogenic alpha-amylase Novamyl into a CGTase.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11796168
Journal J Biotechnol
Year 2002
Volume 94
Pages 137-55
Authors van der Maarel MJ, van der Veen B, Uitdehaag JC, Leemhuis H, Dijkhuizen L
Title Properties and applications of starch-converting enzymes of the alpha-amylase family.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 12581203
Journal Eur J Biochem
Year 2003
Volume 270
Pages 635-45
Authors Janecek S, Svensson B, MacGregor EA
Title Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 12890607
Journal J Biotechnol
Year 2003
Volume 103
Pages 203-12
Authors Leemhuis H, Kragh KM, Dijkstra BW, Dijkhuizen L
Title Engineering cyclodextrin glycosyltransferase into a starch hydrolase with a high exo-specificity.
Related PDB
Related UniProtKB

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.

Created Updated
2007-01-16 2009-02-26