EzCatDB: M00193
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DB codeM00193
RLCP classification1.30.36000.3 : Hydrolysis
CATH domainDomain 12.60.40.10 : Immunoglobulin-like
Domain 23.20.20.80 : TIM BarrelCatalytic domain
Domain 31.-.-.-
Domain 42.60.40.1180 : Immunoglobulin-like
E.C.3.2.1.135
CSA1bvz

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,M00112,T00063,T00065,T00067,T00245
2.60.40.1180 : Immunoglobulin-likeM00113,T00307,D00165,D00176,D00664,D00665,D00863,D00864,M00112,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,M00112,M00346,T00057,T00062,T00063,T00066,T00067

Enzyme Name
UniProtKBKEGG

Q08751P38940
Protein nameNeopullulanase 2Neopullulanaseneopullulanase
pullulanase II
SynonymsEC 3.2.1.135
Alpha-amylase II
TVA II
EC 3.2.1.135
PfamPF00128 (Alpha-amylase)
PF02806 (Alpha-amylase_C)
PF02903 (Alpha-amylase_N)
[Graphical view]
PF00128 (Alpha-amylase)
PF02903 (Alpha-amylase_N)
[Graphical view]
CAZyGH13 (Glycoside Hydrolase Family)
GH13 (Glycoside Hydrolase Family)


UniProtKB:Accession NumberQ08751P38940
Entry nameNEPU2_THEVUNEPU_BACST
ActivityHydrolysis of pullulan to panose (6-alpha-D- glucosylmaltose).Hydrolysis of pullulan to panose (6-alpha-D- glucosylmaltose).
SubunitMonomer.Dimer.
Subcellular location

CofactorBinds 1 calcium ion per subunit.Binds 1 calcium ion per subunit.

Compound table: links to PDB-related databases & PoSSuM

CofactorsSubstratesProducts
KEGG-idC00076C00480C00001C00480C00713
CompoundCalciumPullulanH2OPullulanPanose
Typedivalent metal (Ca2+, Mg2+)polysaccharideH2Opolysaccharidepolysaccharide
ChEBI29108

15377


PubChem271

962
22247451

44630447
             
1bvzA01UnboundUnbound UnboundUnbound
1bvzB01UnboundUnbound UnboundUnbound
1g1yA01UnboundUnbound UnboundUnbound
1g1yB01UnboundUnbound UnboundUnbound
1jf5A01UnboundUnbound UnboundUnbound
1jf5B01UnboundUnbound UnboundUnbound
1jf6A01UnboundUnbound UnboundUnbound
1jf6B01UnboundUnbound UnboundUnbound
1ji2A01UnboundUnbound UnboundUnbound
1ji2B01UnboundUnbound UnboundUnbound
1jibA01UnboundUnbound UnboundUnbound
1jibB01UnboundUnbound UnboundUnbound
1jl8A01UnboundUnbound UnboundUnbound
1jl8B01UnboundUnbound UnboundUnbound
1vb9A01UnboundUnbound UnboundUnbound
1vb9B01UnboundUnbound UnboundUnbound
1vfkA01UnboundUnbound UnboundUnbound
1vfkB01UnboundUnbound UnboundUnbound
1vfmA01UnboundUnbound UnboundUnbound
1vfmB01UnboundUnbound UnboundUnbound
1vfoA01UnboundUnbound UnboundUnbound
1vfoB01UnboundUnbound UnboundUnbound
1vfuA01UnboundUnbound UnboundUnbound
1vfuB01UnboundUnbound UnboundUnbound
1wzkA01UnboundUnbound UnboundUnbound
1wzkB01UnboundUnbound UnboundUnbound
1wzlA01UnboundUnbound UnboundUnbound
1wzlB01UnboundUnbound UnboundUnbound
1wzmA01UnboundUnbound UnboundUnbound
1wzmB01UnboundUnbound UnboundUnbound
1j0hA01UnboundUnbound UnboundUnbound
1j0hB01UnboundUnbound UnboundUnbound
1j0iA01UnboundUnbound UnboundUnbound
1j0iB01UnboundUnbound UnboundUnbound
1j0jA01UnboundUnbound UnboundUnbound
1j0jB01UnboundUnbound UnboundUnbound
1j0kA01UnboundUnbound UnboundUnbound
1j0kB01UnboundUnbound UnboundUnbound
1bvzA02UnboundUnbound UnboundUnbound
1bvzB02UnboundUnbound UnboundUnbound
1g1yA02UnboundAnalogue:BCD UnboundUnbound
1g1yB02UnboundAnalogue:BCD UnboundUnbound
1jf5A02Bound:_CAUnbound UnboundUnbound
1jf5B02Bound:_CAUnbound UnboundUnbound
1jf6A02Bound:_CAUnbound UnboundUnbound
1jf6B02Bound:_CAUnbound UnboundUnbound
1ji2A02Bound:_CAUnbound UnboundUnbound
1ji2B02Bound:_CAUnbound UnboundUnbound
1jibA02UnboundAnalogue:MTT UnboundUnbound
1jibB02UnboundAnalogue:MTT UnboundUnbound
1jl8A02UnboundAnalogue:BCD UnboundUnbound
1jl8B02UnboundAnalogue:BCD UnboundUnbound
1vb9A02Bound:_CAAnalogue:GLC-GLC-GLC-GLC-GLC-GLC UnboundUnbound
1vb9B02Bound:_CAAnalogue:GLC-GLC-GLC-GLC-GLC-GLC UnboundUnbound
1vfkA02Bound:_CAUnbound Analogue:GLC-GLCAnalogue:GLC
1vfkB02Bound:_CAUnbound Analogue:GLC-GLCAnalogue:GLC
1vfmA02Bound:_CAAnalogue:GLC-GLC-GLC-GLC-GLC-GLC UnboundUnbound
1vfmB02Bound:_CAAnalogue:GLC-GLC-GLC-GLC-GLC-GLC UnboundUnbound
1vfoA02Bound:_CAAnalogue:GLC-GLC-GLC-GLC-GLC-GLC-GLC UnboundUnbound
1vfoB02Bound:_CAAnalogue:GLC-GLC-GLC-GLC-GLC-GLC-GLC UnboundUnbound
1vfuA02Bound:_CAAnalogue:GLC-GLC-GLC-GLC-GLC-GLC-GLC-GLC UnboundUnbound
1vfuB02Bound:_CAAnalogue:GLC-GLC-GLC-GLC-GLC-GLC-GLC UnboundUnbound
1wzkA02Bound:_CAUnbound UnboundUnbound
1wzkB02Bound:_CAUnbound UnboundUnbound
1wzlA02Bound:_CAUnbound UnboundUnbound
1wzlB02Bound:_CAUnbound UnboundUnbound
1wzmA02Bound:_CAUnbound UnboundUnbound
1wzmB02Bound:_CAUnbound UnboundUnbound
1j0hA02Bound:_CAUnbound UnboundUnbound
1j0hB02Bound:_CAUnbound UnboundUnbound
1j0iA02UnboundUnbound Bound:GLC-GLC-GLCUnbound
1j0iB02UnboundUnbound Bound:GLC-GLC-GLCUnbound
1j0jA02UnboundAnalogue:GLC-GLC-GLC-GLC UnboundUnbound
1j0jB02UnboundAnalogue:GLC-GLC-GLC-GLC UnboundUnbound
1j0kA02UnboundAnalogue:GLC-GLC-GLC UnboundUnbound
1j0kB02UnboundAnalogue:GLC-GLC-GLC UnboundUnbound
1bvzA03UnboundUnbound UnboundUnbound
1bvzB03UnboundUnbound UnboundUnbound
1g1yA03UnboundUnbound UnboundUnbound
1g1yB03UnboundUnbound UnboundUnbound
1jf5A03UnboundUnbound UnboundUnbound
1jf5B03UnboundUnbound UnboundUnbound
1jf6A03UnboundUnbound UnboundUnbound
1jf6B03UnboundUnbound UnboundUnbound
1ji2A03UnboundUnbound UnboundUnbound
1ji2B03UnboundUnbound UnboundUnbound
1jibA03UnboundUnbound UnboundUnbound
1jibB03UnboundUnbound UnboundUnbound
1jl8A03UnboundUnbound UnboundUnbound
1jl8B03UnboundUnbound UnboundUnbound
1vb9A03UnboundUnbound UnboundUnbound
1vb9B03UnboundUnbound UnboundUnbound
1vfkA03UnboundUnbound UnboundUnbound
1vfkB03UnboundUnbound UnboundUnbound
1vfmA03UnboundUnbound UnboundUnbound
1vfmB03UnboundUnbound UnboundUnbound
1vfoA03UnboundUnbound UnboundUnbound
1vfoB03UnboundUnbound UnboundUnbound
1vfuA03UnboundUnbound UnboundUnbound
1vfuB03UnboundUnbound UnboundUnbound
1wzkA03UnboundUnbound UnboundUnbound
1wzkB03UnboundUnbound UnboundUnbound
1wzlA03UnboundUnbound UnboundUnbound
1wzlB03UnboundUnbound UnboundUnbound
1wzmA03UnboundUnbound UnboundUnbound
1wzmB03UnboundUnbound UnboundUnbound
1j0hA03UnboundUnbound UnboundUnbound
1j0hB03UnboundUnbound UnboundUnbound
1j0iA03UnboundUnbound UnboundUnbound
1j0iB03UnboundUnbound UnboundUnbound
1j0jA03UnboundUnbound UnboundUnbound
1j0jB03UnboundUnbound UnboundUnbound
1j0kA03UnboundUnbound UnboundUnbound
1j0kB03UnboundUnbound UnboundUnbound
1bvzA04UnboundUnbound UnboundUnbound
1bvzB04UnboundUnbound UnboundUnbound
1g1yA04UnboundUnbound UnboundUnbound
1g1yB04UnboundUnbound UnboundUnbound
1jf5A04UnboundUnbound UnboundUnbound
1jf5B04UnboundUnbound UnboundUnbound
1jf6A04UnboundUnbound UnboundUnbound
1jf6B04UnboundUnbound UnboundUnbound
1ji2A04UnboundUnbound UnboundUnbound
1ji2B04UnboundUnbound UnboundUnbound
1jibA04UnboundUnbound UnboundUnbound
1jibB04UnboundUnbound UnboundUnbound
1jl8A04UnboundUnbound UnboundUnbound
1jl8B04UnboundUnbound UnboundUnbound
1vb9A04UnboundUnbound UnboundUnbound
1vb9B04UnboundUnbound UnboundUnbound
1vfkA04UnboundUnbound UnboundUnbound
1vfkB04UnboundUnbound UnboundUnbound
1vfmA04UnboundUnbound UnboundUnbound
1vfmB04UnboundUnbound UnboundUnbound
1vfoA04UnboundUnbound UnboundUnbound
1vfoB04UnboundUnbound UnboundUnbound
1vfuA04UnboundUnbound UnboundUnbound
1vfuB04UnboundUnbound UnboundUnbound
1wzkA04UnboundUnbound UnboundUnbound
1wzkB04UnboundUnbound UnboundUnbound
1wzlA04UnboundUnbound UnboundUnbound
1wzlB04UnboundUnbound UnboundUnbound
1wzmA04UnboundUnbound UnboundUnbound
1wzmB04UnboundUnbound UnboundUnbound
1j0hA04UnboundUnbound UnboundUnbound
1j0hB04UnboundUnbound UnboundUnbound
1j0iA04UnboundUnbound UnboundUnbound
1j0iB04UnboundUnbound UnboundUnbound
1j0jA04UnboundUnbound UnboundUnbound
1j0jB04UnboundUnbound UnboundUnbound
1j0kA04UnboundUnbound UnboundUnbound
1j0kB04UnboundUnbound UnboundUnbound

Active-site residues
resource
Swiss-prot;Q08751, P38940 & literature [9], [11], [20]
pdbCatalytic residuesCofactor-binding residuescomment
           
1bvzA01 
 
 
1bvzB01 
 
 
1g1yA01 
 
 
1g1yB01 
 
 
1jf5A01 
 
 
1jf5B01 
 
 
1jf6A01 
 
 
1jf6B01 
 
 
1ji2A01 
 
 
1ji2B01 
 
 
1jibA01 
 
 
1jibB01 
 
 
1jl8A01 
 
 
1jl8B01 
 
 
1vb9A01 
 
 
1vb9B01 
 
 
1vfkA01 
 
 
1vfkB01 
 
 
1vfmA01 
 
 
1vfmB01 
 
 
1vfoA01 
 
 
1vfoB01 
 
 
1vfuA01 
 
 
1vfuB01 
 
 
1wzkA01 
 
 
1wzkB01 
 
 
1wzlA01 
 
 
1wzlB01 
 
 
1wzmA01 
 
 
1wzmB01 
 
 
1j0hA01 
 
 
1j0hB01 
 
 
1j0iA01 
 
 
1j0iB01 
 
 
1j0jA01 
 
 
1j0jB01 
 
 
1j0kA01 
 
 
1j0kB01 
 
 
1bvzA02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
 
1bvzB02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
 
1g1yA02ASP 325;       ;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant E354A
1g1yB02ASP 325;       ;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant E354A
1jf5A02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant F286A
1jf5B02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant F286A
1jf6A02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant F286Y
1jf6B02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant F286Y
1ji2A02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
 
1ji2B02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
 
1jibA02       ;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N
1jibB02       ;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N
1jl8A02       ;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N
1jl8B02       ;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N
1vb9A02       ;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N
1vb9B02       ;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N
1vfkA02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
 
1vfkB02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
 
1vfmA02       ;GLU 354;       
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N, D421N
1vfmB02       ;GLU 354;       
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N, D421N
1vfoA02       ;GLU 354;       
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N, D421N
1vfoB02       ;GLU 354;       
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N, D421N
1vfuA02       ;GLU 354;       
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N, D421N
1vfuB02       ;GLU 354;       
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D325N, D421N
1wzkA02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D465N
1wzkB02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant D465N
1wzlA02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant R469L
1wzlB02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant R469L
1wzmA02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant R469K
1wzmB02ASP 325;GLU 354;ASP 421
ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
mutant R469K
1j0hA02ASP 328;GLU 357;ASP 424
ASN 147;ASN 149;       ;SER 153;GLY 172;ASP 174(Calcium binding)
 
1j0hB02ASP 328;GLU 357;ASP 424
ASN 147;ASN 149;       ;SER 153;GLY 172;ASP 174(Calcium binding)
 
1j0iA02ASP 328;GLU 357;ASP 424
ASN 147;ASN 149;       ;SER 153;GLY 172;ASP 174(Calcium binding)
 
1j0iB02ASP 328;GLU 357;ASP 424
ASN 147;ASN 149;       ;SER 153;GLY 172;ASP 174(Calcium binding)
 
1j0jA02ASP 328;       ;ASP 424
ASN 147;ASN 149;       ;SER 153;GLY 172;ASP 174(Calcium binding)
mutantE357Q
1j0jB02ASP 328;       ;ASP 424
ASN 147;ASN 149;       ;SER 153;GLY 172;ASP 174(Calcium binding)
mutantE357Q
1j0kA02ASP 328;       ;ASP 424
ASN 147;ASN 149;       ;SER 153;GLY 172;ASP 174(Calcium binding)
mutantE357Q
1j0kB02ASP 328;       ;ASP 424
ASN 147;ASN 149;       ;SER 153;GLY 172;ASP 174(Calcium binding)
mutantE357Q
1bvzA03 
 
 
1bvzB03 
 
 
1g1yA03 
 
 
1g1yB03 
 
 
1jf5A03 
 
 
1jf5B03 
 
 
1jf6A03 
 
 
1jf6B03 
 
 
1ji2A03 
 
 
1ji2B03 
 
 
1jibA03 
 
 
1jibB03 
 
 
1jl8A03 
 
 
1jl8B03 
 
 
1vb9A03 
 
 
1vb9B03 
 
 
1vfkA03 
 
 
1vfkB03 
 
 
1vfmA03 
 
 
1vfmB03 
 
 
1vfoA03 
 
 
1vfoB03 
 
 
1vfuA03 
 
 
1vfuB03 
 
 
1wzkA03 
 
 
1wzkB03 
 
 
1wzlA03 
 
 
1wzlB03 
 
 
1wzmA03 
 
 
1wzmB03 
 
 
1j0hA03 
 
 
1j0hB03 
 
 
1j0iA03 
 
 
1j0iB03 
 
 
1j0jA03 
 
 
1j0jB03 
 
 
1j0kA03 
 
 
1j0kB03 
 
 
1bvzA04 
 
 
1bvzB04 
 
 
1g1yA04 
 
 
1g1yB04 
 
 
1jf5A04 
 
 
1jf5B04 
 
 
1jf6A04 
 
 
1jf6B04 
 
 
1ji2A04 
 
 
1ji2B04 
 
 
1jibA04 
 
 
1jibB04 
 
 
1jl8A04 
 
 
1jl8B04 
 
 
1vb9A04 
 
 
1vb9B04 
 
 
1vfkA04 
 
 
1vfkB04 
 
 
1vfmA04 
 
 
1vfmB04 
 
 
1vfoA04 
 
 
1vfoB04 
 
 
1vfuA04 
 
 
1vfuB04 
 
 
1wzkA04 
 
 
1wzkB04 
 
 
1wzlA04 
 
 
1wzlB04 
 
 
1wzmA04 
 
 
1wzmB04 
 
 
1j0hA04 
 
 
1j0hB04 
 
 
1j0iA04 
 
 
1j0iB04 
 
 
1j0jA04 
 
 
1j0jB04 
 
 
1j0kA04 
 
 
1j0kB04 
 
 

References for Catalytic Mechanism
ReferencesSectionsNo. of steps in catalysis
[5]p.146-150
[10]Fig.2, p.170
[12]Fig.2
[22]FIG.5, p.31038

references
[1]
PubMed ID1388153
JournalJ Biol Chem
Year1992
Volume267
Pages18447-52
AuthorsTakata H, Kuriki T, Okada S, Takesada Y, Iizuka M, Minamiura N, Imanaka T
TitleAction of neopullulanase. Neopullulanase catalyzes both hydrolysis and transglycosylation at alpha-(1----4)- and alpha-(1----6)-glucosidic linkages.
[2]
PubMed ID8136030
JournalJ Protein Chem
Year1993
Volume12
Pages791-805
AuthorsJespersen HM, MacGregor EA, Henrissat B, Sierks MR, Svensson B
TitleStarch- and glycogen-debranching and branching enzymes: prediction of structural features of the catalytic (beta/alpha)8-barrel domain and evolutionary relationship to other amylolytic enzymes.
[3]
PubMed ID8087809
JournalCarbohydr Res
Year1994
Volume261
Pages157-62
AuthorsTonozuka T, Sakai H, Ohta T, Sakano Y
TitleA convenient enzymatic synthesis of 4(2)-alpha-isomaltosylisomaltose using Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II).
[4]
PubMed ID7822101
JournalInt J Pept Protein Res
Year1994
Volume44
Pages245-52
AuthorsHansen G, Heese O, Hohne WE, Hofemeister B
Titlealpha-Amylases from Thermoactinomyces vulgaris: characteristics, primary structure and structure prediction.
[5]
PubMed ID8018865
JournalPlant Mol Biol
Year1994
Volume25
Pages141-57
AuthorsSvensson B
TitleProtein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity, and stability.
[6]
PubMed ID8695646
JournalBiochim Biophys Acta
Year1996
Volume1295
Pages195-200
AuthorsLamminmaki U, Vihinen M
TitleStructural consequences of neopullulanase mutations.
[7]
PubMed ID8663322
JournalJ Biol Chem
Year1996
Volume271
Pages17321-9
AuthorsKuriki T, Kaneko H, Yanase M, Takata H, Shimada J, Handa S, Takada T, Umeyama H, Okada S
TitleControlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center.
[8]
PubMed ID10403384
JournalFEBS Lett
Year1999
Volume453
Pages100-6
AuthorsSaab-Rincon G, del-Rio G, Santamaria RI, Lopez-Munguia A, Soberon X
TitleIntroducing transglycosylation activity in a liquefying alpha-amylase.
[9]
CommentsX-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID99241045
PubMed ID10222200
JournalJ Mol Biol
Year1999
Volume287
Pages907-21
AuthorsKamitori S, Kondo S, Okuyama K, Yokota T, Shimura Y, Tonozuka T, Sakano Y
TitleCrystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution.
Related PDB1bvz
Related UniProtKBQ08751
[10]
PubMed ID10825529
JournalBiochim Biophys Acta
Year2000
Volume1478
Pages165-85
AuthorsPark KH, Kim TJ, Cheong TK, Kim JW, Oh BH, Svensson B
TitleStructure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family.
[11]
PubMed ID11210138
JournalBiosci Biotechnol Biochem
Year2000
Volume64
Pages2692-5
AuthorsIchikawa K, Tonozuka T, Yokota T, Shimura Y, Sakano Y
TitleAnalysis of catalytic residues of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) by site-directed mutagenesis.
[12]
PubMed ID11257505
JournalBiochim Biophys Acta
Year2001
Volume1546
Pages1-20
AuthorsMacGregor EA, Janecek S, Svensson B
TitleRelationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
[13]
CommentsX-ray crystallography
PubMed ID11330677
JournalBiosci Biotechnol Biochem
Year2001
Volume65
Pages619-26
AuthorsYokota T, Tonozuka T, Shimura Y, Ichikawa K, Kamitori S, Sakano Y
TitleStructures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues.
Related PDB1jib,1jl8
[14]
CommentsX-ray crystallography
PubMed ID11527532
JournalCarbohydr Res
Year2001
Volume334
Pages309-13
AuthorsOhtaki A, Kondo S, Shimura Y, Tonozuka T, Sakano Y, Kamitori S
TitleRole of Phe286 in the recognition mechanism of cyclomaltooligosaccharides (cyclodextrins) by Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structures of the mutant TVAIIs, F286A and F286Y, and kinetic analyses of the Phe286-replaced mutant TVAIIs.
Related PDB1jf5,1jf6
[15]
CommentsX-ray crystallography
PubMed ID11226882
JournalJ Biochem (Tokyo)
Year2001
Volume129
Pages423-8
AuthorsKondo S, Ohtaki A, Tonozuka T, Sakano Y, Kamitori S
TitleStudies on the hydrolyzing mechanism for cyclodextrins of Thermoactinomyces vulgaris R-47 alpha-amylase 2 (TVAII). X-ray structure of the mutant E354A complexed with beta-cyclodextrin, and kinetic analyses on cyclodextrins.
Related PDB1g1y
[16]
PubMed ID11834127
JournalBiotechnol Appl Biochem
Year2002
Volume35
Pages27-34
AuthorsCheong KA, Kim TJ, Yoon JW, Park CS, Lee TS, Kim YB, Park KH, Kim JW
TitleCatalytic activities of intracellular dimeric neopullulanase on cyclodextrin, acarbose and maltose.
[17]
PubMed ID11923309
JournalJ Biol Chem
Year2002
Volume277
Pages21891-7
AuthorsLee HS, Kim MS, Cho HS, Kim JI, Kim TJ, Choi JH, Park C, Lee HS, Oh BH, Park KH
TitleCyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other.
[18]
CommentsX-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID22047855
PubMed ID12051850
JournalJ Mol Biol
Year2002
Volume318
Pages443-53
AuthorsKamitori S, Abe A, Ohtaki A, Kaji A, Tonozuka T, Sakano Y
TitleCrystal structures and structural comparison of Thermoactinomyces vulgaris R-47 alpha-amylase 1 (TVAI) at 1.6 A resolution and alpha-amylase 2 (TVAII) at 2.3 A resolution.
Related PDB1ji2
Related UniProtKBQ08751
[19]
PubMed ID12860426
JournalCarbohydr Res
Year2003
Volume338
Pages1553-8
AuthorsOhtaki A, Iguchi A, Mizuno M, Tonozuka T, Sakano Y, Kamitori S
TitleMutual conversion of substrate specificities of Thermoactinomyces vulgaris R-47 alpha-amylases TVAI and TVAII by site-directed mutagenesis.
[20]
CommentsX-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
PubMed ID12547200
JournalJ Mol Biol
Year2003
Volume326
Pages177-88
AuthorsHondoh H, Kuriki T, Matsuura Y
TitleThree-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase.
Related PDB1j0h,1j0i,1j0j,1j0k
Related UniProtKBP38940
[21]
CommentsX-ray crystallography
PubMed ID15182368
JournalEur J Biochem
Year2004
Volume271
Pages2530-8
AuthorsMizuno M, Tonozuka T, Uechi A, Ohtaki A, Ichikawa K, Kamitori S, Nishikawa A, Sakano Y
TitleThe crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product.
Related PDB1vb9
[22]
CommentsX-ray crystallography
PubMed ID15138257
JournalJ Biol Chem
Year2004
Volume279
Pages31033-40
AuthorsOhtaki A, Mizuno M, Tonozuka T, Sakano Y, Kamitori S
TitleComplex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism.
Related PDB1vfk,1vfm,1vfo,1vfu

comments
This enzyme belongs to the glycosidase family-13.
Although this enzyme binds a calcium ion, it is distant from the active site and not involved in catalysis.
According to the literature [10] & [22], this enzyme has a similar catalytic mechanism to that of alpha-amylase (D00165 in EzCatDB).
Asp325 of 1bvz (PDB) acts as a nucleophile, whereas Glu354 acts as an acid-base. Asp421 probably stabilizes transition state.
(1) Glu354 initiates the reaction by protonating O4 atom, giving an oxocarbonium ion-like transition state.
(2) Asp325 makes a nucleophilic attack on the C1 atom to form glycosyl-enzyme intermediate.
(3) Glu354 acts as a general base to activate a water.
(4) The activated water attacks on the intermediate to complete the hydrolysis.

createdupdated
2005-04-212009-02-26


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