EzCatDB: D00176

DB codeD00176
RLCP classification1.30.36000.3
CATH domainDomain 13.20.20.80Catalytic domain
Domain 22.60.40.1180
E.C.3.2.1.60
CSA2amg

CATH domainRelated DB codes (homologues)
2.60.40.1180M00113,T00307,D00165,D00664,D00665,D00863,D00864,M00112,M00193,M00314,T00057,T00062,T00067
3.20.20.80S00202,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,D00501,D00502,D00503,D00844,D00861,D00864,M00026,M00112,M00193,M00346,T00057,T00062,T00063,T00066,T00067

Enzyme Name
Swiss-protKEGG

P13507
Protein nameGlucan 1,4-alpha-maltotetraohydrolaseglucan 1,4-alpha-maltotetraohydrolase
exo-maltotetraohydrolase
1,4-alpha-D-glucan maltotetraohydrolase
SynonymsG4-amylase
EC 3.2.1.60
Maltotetraose-forming amylase
Exo-maltotetraohydrolase
Maltotetraose-forming exo-amylase


Swiss-prot:Accession NumberP13507
Entry nameAMT4_PSEST
ActivityHydrolysis of (1->4)-alpha-D-glucosidic linkages in amylaceous polysaccharides, to remove successive maltotetraose residues from the non-reducing chain ends.
SubunitMonomer.
Subcellular locationSecreted.
CofactorBinds 2 calcium ions per subunit.


CofactorsSubstratesProducts
KEGG-idC00076C00657C00001C02052C01935
CompoundCalciumAmylaceous polysaccharideH2OMaltotetraoseMaltodextrin
Typedivalent metal (Ca2+, Mg2+)polysaccharideH2Opolysaccharidepolysaccharide
1amgA01Bound:2x_CAUnbound
UnboundUnbound
1gcyA01Bound:2x_CAUnbound
UnboundUnbound
1jdaA01Bound:2x_CAUnbound
UnboundUnbound
1jdcA01Bound:2x_CAUnbound
Bound:GLC-GLC-GLC-GLCUnbound
1jddA01Bound:2x_CAUnbound
Bound:GLC-GLC-GLC-GLCUnbound
1qi3A01Bound:2x_CAUnbound
Bound:MTTUnbound
1qi4A01Bound:2x_CAUnbound
Bound:MTTUnbound
1qi5A01Bound:2x_CAUnbound
Bound:MTTUnbound
1qpkA01Bound:2x_CAUnbound
Bound:MTTUnbound
2amgA01Bound:2x_CAUnbound
UnboundUnbound
1amgA02UnboundUnbound
UnboundUnbound
1gcyA02UnboundUnbound
UnboundUnbound
1jdaA02UnboundUnbound
UnboundUnbound
1jdcA02UnboundUnbound
UnboundUnbound
1jddA02UnboundUnbound
UnboundUnbound
1qi3A02UnboundUnbound
UnboundUnbound
1qi4A02UnboundUnbound
UnboundUnbound
1qi5A02UnboundUnbound
UnboundUnbound
1qpkA02UnboundUnbound
UnboundUnbound
2amgA02UnboundUnbound
UnboundUnbound

Active-site residues
resource
Swiss-prot;P13507 & Literature [5], [6], [8]
pdbCatalytic residuesCofactor-binding residuescomment
1amgA01ASP 193;GLU 219;ASP 294
ASN 116;ASP 151;ASP 154;ASP 162;GLY 197(calcium-1);ASP 1;GLN 2;HIS 13;ASP 16;GLU 17(calcium-2)

1gcyA01ASP 193;GLU 219;ASP 294
ASN 116;ASP 151;ASP 154;ASP 162;GLY 197(calcium-1);ASP 1;GLN 2;HIS 13;ASP 16;GLU 17(calcium-2)

1jdaA01ASP 193;       ;ASP 294
ASN 116;ASP 151;ASP 154;ASP 162;GLY 197(calcium-1);ASP 1;GLN 2;HIS 13;ASP 16;GLU 17(calcium-2)
mutant E219Q
1jdcA01ASP 193;       ;ASP 294
ASN 116;ASP 151;ASP 154;ASP 162;GLY 197(calcium-1);ASP 1;GLN 2;HIS 13;ASP 16;GLU 17(calcium-2)
mutant E219Q
1jddA01ASP 193;       ;ASP 294
ASN 116;ASP 151;ASP 154;ASP 162;GLY 197(calcium-1);ASP 1;GLN 2;HIS 13;ASP 16;GLU 17(calcium-2)
mutant E219Q
1qi3A01       ;GLU 219;ASP 294
ASN 116;ASP 151;ASP 154;ASP 162;GLY 197(calcium-1);ASP 1;GLN 2;HIS 13;ASP 16;GLU 17(calcium-2)
mutant D193N
1qi4A01ASP 193;       ;ASP 294
ASN 116;ASP 151;ASP 154;ASP 162;GLY 197(calcium-1);ASP 1;GLN 2;HIS 13;ASP 16;GLU 17(calcium-2)
mutant E219G
1qi5A01ASP 193;GLU 219;       
ASN 116;ASP 151;ASP 154;ASP 162;GLY 197(calcium-1);ASP 1;GLN 2;HIS 13;ASP 16;GLU 17(calcium-2)
mutant D294N
1qpkA01       ;GLU 219;ASP 294
ASN 116;ASP 151;ASP 154;ASP 162;GLY 197(calcium-1);ASP 1;GLN 2;HIS 13;ASP 16;GLU 17(calcium-2)
mutant D193G
2amgA01ASP 193;GLU 219;ASP 294
ASN 116;ASP 151;ASP 154;ASP 162;GLY 197(calcium-1);ASP 1;GLN 2;HIS 13;ASP 16;GLU 17(calcium-2)

1amgA02


1gcyA02


1jdaA02


1jdcA02


1jddA02


1qi3A02


1qi4A02


1qi5A02


1qpkA02


2amgA02



References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[6]p.625
[8]Fig.3, p.822-823

references
[1]
CommentsNUCLEOTIDE SEQUENCE
PubMed ID2676600
JournalFEBS Lett
Year1989
Volume255
Pages37-41
AuthorsZhou JH, Baba T, Takano T, Kobayashi S, Arai Y
TitleNucleotide sequence of the maltotetraohydrolase gene from Pseudomonas saccharophila.
[2]
CommentsNUCLEOTIDE SEQUENCE
PubMed ID2646279
JournalJ Bacteriol
Year1989
Volume171
Pages1333-9
AuthorsFujita M, Torigoe K, Nakada T, Tsusaki K, Kubota M, Sakai S, Tsujisaka Y
TitleCloning and nucleotide sequence of the gene (amyP) for maltotetraose-forming amylase from Pseudomonas stutzeri MO-19.
Related Swiss-protP13507
[3]
PubMed ID1368535
JournalAgric Biol Chem
Year1990
Volume54
Pages737-43
AuthorsNakada T, Kubota M, Sakai S, Tsujisaka Y
TitlePurification and characterization of two forms of maltotetraose-forming amylase from Pseudomonas stutzeri.
[4]
PubMed ID1596923
JournalCarbohydr Res
Year1992
Volume223
Pages255-61
AuthorsZhou JH, Baba T, Takano T, Kobayashi S, Arai Y
TitleProperties of the enzyme expressed by the Pseudomonas saccharophila maltotetraohydrolase gene (mta) in Escherichia coli.
[5]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND REVISIONS TO 286-302.
Medline ID97271999
PubMed ID9126844
JournalJ Mol Biol
Year1997
Volume267
Pages661-72
AuthorsMorishita Y, Hasegawa K, Matsuura Y, Katsube Y, Kubota M, Sakai S
TitleCrystal structure of a maltotetraose-forming exo-amylase from Pseudomonas stutzeri.
Related PDB1amg
Related Swiss-protP13507
[6]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF VARIANT GLN-240.
Medline ID97428332
PubMed ID9281429
JournalJ Mol Biol
Year1997
Volume271
Pages619-28
AuthorsYoshioka Y, Hasegawa K, Matsuura Y, Katsube Y, Kubota M
TitleCrystal structures of a mutant maltotetraose-forming exo-amylase cocrystallized with maltopentaose.
Related PDB1jda,1jdc,1jdd
Related Swiss-protP13507
[7]
PubMed ID9827329
JournalExtremophiles
Year1998
Volume2
Pages401-7
AuthorsKobayashi H, Takaki Y, Kobata K, Takami H, Inoue A
TitleCharacterization of alpha-maltotetraohydrolase produced by Pseudomonas sp. MS300 isolated from the deepest site of the mariana trench.
[8]
CommentsX-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF VARIANTS.
Medline ID20027472
PubMed ID10556241
JournalProtein Eng
Year1999
Volume12
Pages819-24
AuthorsHasegawa K, Kubota M, Matsuura Y
TitleRoles of catalytic residues in alpha-amylases as evidenced by the structures of the product-complexed mutants of a maltotetraose-forming amylase.
Related PDB1qi3,1qi4,1qi5,1qpk
Related Swiss-protP13507
[9]
CommentsX-ray crystallography
PubMed ID11272837
JournalBiosci Biotechnol Biochem
Year2001
Volume65
Pages222-5
AuthorsMezaki Y, Katsuya Y, Kubota M, Matsuura Y
TitleCrystallization and structural analysis of intact maltotetraose-forming exo-amylase from Pseudomonas stutzeri.
Related PDB1gcy

comments
This enzyme belongs to the glycosyl hydrolase family-13, along with alpha-amylase (D00165 in EzCatDB).
Although this enzyme binds two calcium ions, they are not involved in catalysis.
Since this enzyme has got a similar catalytic site to that of alpha-amylase (D00165 in EzCatDB), it must have a similar catalytic mechanism.

createdupdated
2004-05-102009-02-26


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 2010)
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)

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