DB code: M00193

RLCP classification 1.30.36000.3 : Hydrolysis
CATH domain 2.60.40.10 : Immunoglobulin-like
3.20.20.80 : TIM Barrel Catalytic domain
1.-.-.- :
2.60.40.1180 : Immunoglobulin-like
E.C. 3.2.1.135
CSA 1bvz
M-CSA 1bvz
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 T00063 T00065 T00067 T00245
2.60.40.1180 : Immunoglobulin-like M00113 T00307 D00165 D00176 D00664 D00665 D00863 D00864 M00112 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 M00112 M00346 T00057 T00062 T00063 T00066 T00067

Uniprot Enzyme Name
UniprotKB Protein name Synonyms CAZy Pfam
Q08751 Neopullulanase 2
EC 3.2.1.135
Alpha-amylase II
TVA II
CBM34 (Carbohydrate-Binding Module Family 34)
GH13 (Glycoside Hydrolase Family 13)
PF00128 (Alpha-amylase)
PF02806 (Alpha-amylase_C)
PF02903 (Alpha-amylase_N)
[Graphical View]
P38940 Neopullulanase
EC 3.2.1.135
CBM34 (Carbohydrate-Binding Module Family 34)
GH13 (Glycoside Hydrolase Family 13)
PF00128 (Alpha-amylase)
PF02903 (Alpha-amylase_N)
[Graphical View]

KEGG enzyme name
neopullulanase
pullulanase II

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
Q08751 NEPU2_THEVU Hydrolysis of pullulan to panose (6-alpha-D- glucosylmaltose). Monomer. Binds 1 calcium ion per subunit.
P38940 NEPU_BACST Hydrolysis of pullulan to panose (6-alpha-D- glucosylmaltose). Dimer. Binds 1 calcium ion per subunit.

KEGG Pathways
Map code Pathways E.C.

Compound table
Cofactors Substrates Products Intermediates
KEGG-id C00076 C00480 C00001 C00480 C00713
E.C.
Compound Calcium Pullulan H2O Pullulan Panose
Type divalent metal (Ca2+, Mg2+) polysaccharide H2O polysaccharide polysaccharide
ChEBI 29108
29108
15377
15377
PubChem 271
271
22247451
962
22247451
962
44630447
44630447
1bvzA01 Unbound Unbound Unbound Unbound
1bvzB01 Unbound Unbound Unbound Unbound
1g1yA01 Unbound Unbound Unbound Unbound
1g1yB01 Unbound Unbound Unbound Unbound
1jf5A01 Unbound Unbound Unbound Unbound
1jf5B01 Unbound Unbound Unbound Unbound
1jf6A01 Unbound Unbound Unbound Unbound
1jf6B01 Unbound Unbound Unbound Unbound
1ji2A01 Unbound Unbound Unbound Unbound
1ji2B01 Unbound Unbound Unbound Unbound
1jibA01 Unbound Unbound Unbound Unbound
1jibB01 Unbound Unbound Unbound Unbound
1jl8A01 Unbound Unbound Unbound Unbound
1jl8B01 Unbound Unbound Unbound Unbound
1vb9A01 Unbound Unbound Unbound Unbound
1vb9B01 Unbound Unbound Unbound Unbound
1vfkA01 Unbound Unbound Unbound Unbound
1vfkB01 Unbound Unbound Unbound Unbound
1vfmA01 Unbound Unbound Unbound Unbound
1vfmB01 Unbound Unbound Unbound Unbound
1vfoA01 Unbound Unbound Unbound Unbound
1vfoB01 Unbound Unbound Unbound Unbound
1vfuA01 Unbound Unbound Unbound Unbound
1vfuB01 Unbound Unbound Unbound Unbound
1wzkA01 Unbound Unbound Unbound Unbound
1wzkB01 Unbound Unbound Unbound Unbound
1wzlA01 Unbound Unbound Unbound Unbound
1wzlB01 Unbound Unbound Unbound Unbound
1wzmA01 Unbound Unbound Unbound Unbound
1wzmB01 Unbound Unbound Unbound Unbound
1j0hA01 Unbound Unbound Unbound Unbound
1j0hB01 Unbound Unbound Unbound Unbound
1j0iA01 Unbound Unbound Unbound Unbound
1j0iB01 Unbound Unbound Unbound Unbound
1j0jA01 Unbound Unbound Unbound Unbound
1j0jB01 Unbound Unbound Unbound Unbound
1j0kA01 Unbound Unbound Unbound Unbound
1j0kB01 Unbound Unbound Unbound Unbound
1bvzA02 Unbound Unbound Unbound Unbound
1bvzB02 Unbound Unbound Unbound Unbound
1g1yA02 Unbound Analogue:BCD Unbound Unbound
1g1yB02 Unbound Analogue:BCD Unbound Unbound
1jf5A02 Bound:_CA Unbound Unbound Unbound
1jf5B02 Bound:_CA Unbound Unbound Unbound
1jf6A02 Bound:_CA Unbound Unbound Unbound
1jf6B02 Bound:_CA Unbound Unbound Unbound
1ji2A02 Bound:_CA Unbound Unbound Unbound
1ji2B02 Bound:_CA Unbound Unbound Unbound
1jibA02 Unbound Analogue:MTT Unbound Unbound
1jibB02 Unbound Analogue:MTT Unbound Unbound
1jl8A02 Unbound Analogue:BCD Unbound Unbound
1jl8B02 Unbound Analogue:BCD Unbound Unbound
1vb9A02 Bound:_CA Analogue:GLC-GLC-GLC-GLC-GLC-GLC Unbound Unbound
1vb9B02 Bound:_CA Analogue:GLC-GLC-GLC-GLC-GLC-GLC Unbound Unbound
1vfkA02 Bound:_CA Unbound Analogue:GLC-GLC Analogue:GLC
1vfkB02 Bound:_CA Unbound Analogue:GLC-GLC Analogue:GLC
1vfmA02 Bound:_CA Analogue:GLC-GLC-GLC-GLC-GLC-GLC Unbound Unbound
1vfmB02 Bound:_CA Analogue:GLC-GLC-GLC-GLC-GLC-GLC Unbound Unbound
1vfoA02 Bound:_CA Analogue:GLC-GLC-GLC-GLC-GLC-GLC-GLC Unbound Unbound
1vfoB02 Bound:_CA Analogue:GLC-GLC-GLC-GLC-GLC-GLC-GLC Unbound Unbound
1vfuA02 Bound:_CA Analogue:GLC-GLC-GLC-GLC-GLC-GLC-GLC-GLC Unbound Unbound
1vfuB02 Bound:_CA Analogue:GLC-GLC-GLC-GLC-GLC-GLC-GLC Unbound Unbound
1wzkA02 Bound:_CA Unbound Unbound Unbound
1wzkB02 Bound:_CA Unbound Unbound Unbound
1wzlA02 Bound:_CA Unbound Unbound Unbound
1wzlB02 Bound:_CA Unbound Unbound Unbound
1wzmA02 Bound:_CA Unbound Unbound Unbound
1wzmB02 Bound:_CA Unbound Unbound Unbound
1j0hA02 Bound:_CA Unbound Unbound Unbound
1j0hB02 Bound:_CA Unbound Unbound Unbound
1j0iA02 Unbound Unbound Bound:GLC-GLC-GLC Unbound
1j0iB02 Unbound Unbound Bound:GLC-GLC-GLC Unbound
1j0jA02 Unbound Analogue:GLC-GLC-GLC-GLC Unbound Unbound
1j0jB02 Unbound Analogue:GLC-GLC-GLC-GLC Unbound Unbound
1j0kA02 Unbound Analogue:GLC-GLC-GLC Unbound Unbound
1j0kB02 Unbound Analogue:GLC-GLC-GLC Unbound Unbound
1bvzA03 Unbound Unbound Unbound Unbound
1bvzB03 Unbound Unbound Unbound Unbound
1g1yA03 Unbound Unbound Unbound Unbound
1g1yB03 Unbound Unbound Unbound Unbound
1jf5A03 Unbound Unbound Unbound Unbound
1jf5B03 Unbound Unbound Unbound Unbound
1jf6A03 Unbound Unbound Unbound Unbound
1jf6B03 Unbound Unbound Unbound Unbound
1ji2A03 Unbound Unbound Unbound Unbound
1ji2B03 Unbound Unbound Unbound Unbound
1jibA03 Unbound Unbound Unbound Unbound
1jibB03 Unbound Unbound Unbound Unbound
1jl8A03 Unbound Unbound Unbound Unbound
1jl8B03 Unbound Unbound Unbound Unbound
1vb9A03 Unbound Unbound Unbound Unbound
1vb9B03 Unbound Unbound Unbound Unbound
1vfkA03 Unbound Unbound Unbound Unbound
1vfkB03 Unbound Unbound Unbound Unbound
1vfmA03 Unbound Unbound Unbound Unbound
1vfmB03 Unbound Unbound Unbound Unbound
1vfoA03 Unbound Unbound Unbound Unbound
1vfoB03 Unbound Unbound Unbound Unbound
1vfuA03 Unbound Unbound Unbound Unbound
1vfuB03 Unbound Unbound Unbound Unbound
1wzkA03 Unbound Unbound Unbound Unbound
1wzkB03 Unbound Unbound Unbound Unbound
1wzlA03 Unbound Unbound Unbound Unbound
1wzlB03 Unbound Unbound Unbound Unbound
1wzmA03 Unbound Unbound Unbound Unbound
1wzmB03 Unbound Unbound Unbound Unbound
1j0hA03 Unbound Unbound Unbound Unbound
1j0hB03 Unbound Unbound Unbound Unbound
1j0iA03 Unbound Unbound Unbound Unbound
1j0iB03 Unbound Unbound Unbound Unbound
1j0jA03 Unbound Unbound Unbound Unbound
1j0jB03 Unbound Unbound Unbound Unbound
1j0kA03 Unbound Unbound Unbound Unbound
1j0kB03 Unbound Unbound Unbound Unbound
1bvzA04 Unbound Unbound Unbound Unbound
1bvzB04 Unbound Unbound Unbound Unbound
1g1yA04 Unbound Unbound Unbound Unbound
1g1yB04 Unbound Unbound Unbound Unbound
1jf5A04 Unbound Unbound Unbound Unbound
1jf5B04 Unbound Unbound Unbound Unbound
1jf6A04 Unbound Unbound Unbound Unbound
1jf6B04 Unbound Unbound Unbound Unbound
1ji2A04 Unbound Unbound Unbound Unbound
1ji2B04 Unbound Unbound Unbound Unbound
1jibA04 Unbound Unbound Unbound Unbound
1jibB04 Unbound Unbound Unbound Unbound
1jl8A04 Unbound Unbound Unbound Unbound
1jl8B04 Unbound Unbound Unbound Unbound
1vb9A04 Unbound Unbound Unbound Unbound
1vb9B04 Unbound Unbound Unbound Unbound
1vfkA04 Unbound Unbound Unbound Unbound
1vfkB04 Unbound Unbound Unbound Unbound
1vfmA04 Unbound Unbound Unbound Unbound
1vfmB04 Unbound Unbound Unbound Unbound
1vfoA04 Unbound Unbound Unbound Unbound
1vfoB04 Unbound Unbound Unbound Unbound
1vfuA04 Unbound Unbound Unbound Unbound
1vfuB04 Unbound Unbound Unbound Unbound
1wzkA04 Unbound Unbound Unbound Unbound
1wzkB04 Unbound Unbound Unbound Unbound
1wzlA04 Unbound Unbound Unbound Unbound
1wzlB04 Unbound Unbound Unbound Unbound
1wzmA04 Unbound Unbound Unbound Unbound
1wzmB04 Unbound Unbound Unbound Unbound
1j0hA04 Unbound Unbound Unbound Unbound
1j0hB04 Unbound Unbound Unbound Unbound
1j0iA04 Unbound Unbound Unbound Unbound
1j0iB04 Unbound Unbound Unbound Unbound
1j0jA04 Unbound Unbound Unbound Unbound
1j0jB04 Unbound Unbound Unbound Unbound
1j0kA04 Unbound Unbound Unbound Unbound
1j0kB04 Unbound Unbound Unbound Unbound

Reference for Active-site residues
resource references E.C.
Swiss-prot;Q08751, P38940 & literature [9], [11], [20]

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
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
1bvzA02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
1bvzB02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
1g1yA02 ASP 325;;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant E354A
1g1yB02 ASP 325;;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant E354A
1jf5A02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant F286A
1jf5B02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant F286A
1jf6A02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant F286Y
1jf6B02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant F286Y
1ji2A02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
1ji2B02 ASP 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
1vfkA02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding)
1vfkB02 ASP 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
1wzkA02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant D465N
1wzkB02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant D465N
1wzlA02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant R469L
1wzlB02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant R469L
1wzmA02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant R469K
1wzmB02 ASP 325;GLU 354;ASP 421 ASN 143;ASP 145;ASN 148;ASP 149;GLY 169;ASP 171(Calcium binding) mutant R469K
1j0hA02 ASP 328;GLU 357;ASP 424 ASN 147;ASN 149;;SER 153;GLY 172;ASP 174(Calcium binding)
1j0hB02 ASP 328;GLU 357;ASP 424 ASN 147;ASN 149;;SER 153;GLY 172;ASP 174(Calcium binding)
1j0iA02 ASP 328;GLU 357;ASP 424 ASN 147;ASN 149;;SER 153;GLY 172;ASP 174(Calcium binding)
1j0iB02 ASP 328;GLU 357;ASP 424 ASN 147;ASN 149;;SER 153;GLY 172;ASP 174(Calcium binding)
1j0jA02 ASP 328;;ASP 424 ASN 147;ASN 149;;SER 153;GLY 172;ASP 174(Calcium binding) mutantE357Q
1j0jB02 ASP 328;;ASP 424 ASN 147;ASN 149;;SER 153;GLY 172;ASP 174(Calcium binding) mutantE357Q
1j0kA02 ASP 328;;ASP 424 ASN 147;ASN 149;;SER 153;GLY 172;ASP 174(Calcium binding) mutantE357Q
1j0kB02 ASP 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
References Sections No. of steps in catalysis
[5]
p.146-150
[10]
Fig.2, p.170
[12]
Fig.2
[22]
FIG.5, p.31038

References
[1]
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. Neopullulanase catalyzes both hydrolysis and transglycosylation at alpha-(1----4)- and alpha-(1----6)-glucosidic linkages.
Related PDB
Related UniProtKB
[2]
Resource
Comments
Medline ID
PubMed ID 8136030
Journal J Protein Chem
Year 1993
Volume 12
Pages 791-805
Authors Jespersen HM, MacGregor EA, Henrissat B, Sierks MR, Svensson B
Title Starch- 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.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 8087809
Journal Carbohydr Res
Year 1994
Volume 261
Pages 157-62
Authors Tonozuka T, Sakai H, Ohta T, Sakano Y
Title A convenient enzymatic synthesis of 4(2)-alpha-isomaltosylisomaltose using Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II).
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 7822101
Journal Int J Pept Protein Res
Year 1994
Volume 44
Pages 245-52
Authors Hansen G, Heese O, Hohne WE, Hofemeister B
Title alpha-Amylases from Thermoactinomyces vulgaris: characteristics, primary structure and structure prediction.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 8018865
Journal Plant Mol Biol
Year 1994
Volume 25
Pages 141-57
Authors Svensson B
Title Protein engineering in the alpha-amylase family: catalytic mechanism, substrate specificity, and stability.
Related PDB
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 8695646
Journal Biochim Biophys Acta
Year 1996
Volume 1295
Pages 195-200
Authors Lamminmaki U, Vihinen M
Title Structural consequences of neopullulanase mutations.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 8663322
Journal J Biol Chem
Year 1996
Volume 271
Pages 17321-9
Authors Kuriki T, Kaneko H, Yanase M, Takata H, Shimada J, Handa S, Takada T, Umeyama H, Okada S
Title Controlling substrate preference and transglycosylation activity of neopullulanase by manipulating steric constraint and hydrophobicity in active center.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 10403384
Journal FEBS Lett
Year 1999
Volume 453
Pages 100-6
Authors Saab-Rincon G, del-Rio G, Santamaria RI, Lopez-Munguia A, Soberon X
Title Introducing transglycosylation activity in a liquefying alpha-amylase.
Related PDB
Related UniProtKB
[9]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
Medline ID 99241045
PubMed ID 10222200
Journal J Mol Biol
Year 1999
Volume 287
Pages 907-21
Authors Kamitori S, Kondo S, Okuyama K, Yokota T, Shimura Y, Tonozuka T, Sakano Y
Title Crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVAII) hydrolyzing cyclodextrins and pullulan at 2.6 A resolution.
Related PDB 1bvz
Related UniProtKB Q08751
[10]
Resource
Comments
Medline ID
PubMed ID 10825529
Journal Biochim Biophys Acta
Year 2000
Volume 1478
Pages 165-85
Authors Park KH, Kim TJ, Cheong TK, Kim JW, Oh BH, Svensson B
Title Structure, specificity and function of cyclomaltodextrinase, a multispecific enzyme of the alpha-amylase family.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11210138
Journal Biosci Biotechnol Biochem
Year 2000
Volume 64
Pages 2692-5
Authors Ichikawa K, Tonozuka T, Yokota T, Shimura Y, Sakano Y
Title Analysis of catalytic residues of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) by site-directed mutagenesis.
Related PDB
Related UniProtKB
[12]
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
[13]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11330677
Journal Biosci Biotechnol Biochem
Year 2001
Volume 65
Pages 619-26
Authors Yokota T, Tonozuka T, Shimura Y, Ichikawa K, Kamitori S, Sakano Y
Title Structures of Thermoactinomyces vulgaris R-47 alpha-amylase II complexed with substrate analogues.
Related PDB 1jib 1jl8
Related UniProtKB
[14]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11527532
Journal Carbohydr Res
Year 2001
Volume 334
Pages 309-13
Authors Ohtaki A, Kondo S, Shimura Y, Tonozuka T, Sakano Y, Kamitori S
Title Role 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 PDB 1jf5 1jf6
Related UniProtKB
[15]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 11226882
Journal J Biochem (Tokyo)
Year 2001
Volume 129
Pages 423-8
Authors Kondo S, Ohtaki A, Tonozuka T, Sakano Y, Kamitori S
Title Studies 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 PDB 1g1y
Related UniProtKB
[16]
Resource
Comments
Medline ID
PubMed ID 11834127
Journal Biotechnol Appl Biochem
Year 2002
Volume 35
Pages 27-34
Authors Cheong KA, Kim TJ, Yoon JW, Park CS, Lee TS, Kim YB, Park KH, Kim JW
Title Catalytic activities of intracellular dimeric neopullulanase on cyclodextrin, acarbose and maltose.
Related PDB
Related UniProtKB
[17]
Resource
Comments
Medline ID
PubMed ID 11923309
Journal J Biol Chem
Year 2002
Volume 277
Pages 21891-7
Authors Lee HS, Kim MS, Cho HS, Kim JI, Kim TJ, Choi JH, Park C, Lee HS, Oh BH, Park KH
Title Cyclomaltodextrinase, neopullulanase, and maltogenic amylase are nearly indistinguishable from each other.
Related PDB
Related UniProtKB
[18]
Resource
Comments X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
Medline ID 22047855
PubMed ID 12051850
Journal J Mol Biol
Year 2002
Volume 318
Pages 443-53
Authors Kamitori S, Abe A, Ohtaki A, Kaji A, Tonozuka T, Sakano Y
Title Crystal 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 PDB 1ji2
Related UniProtKB Q08751
[19]
Resource
Comments
Medline ID
PubMed ID 12860426
Journal Carbohydr Res
Year 2003
Volume 338
Pages 1553-8
Authors Ohtaki A, Iguchi A, Mizuno M, Tonozuka T, Sakano Y, Kamitori S
Title Mutual conversion of substrate specificities of Thermoactinomyces vulgaris R-47 alpha-amylases TVAI and TVAII by site-directed mutagenesis.
Related PDB
Related UniProtKB
[20]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS).
Medline ID
PubMed ID 12547200
Journal J Mol Biol
Year 2003
Volume 326
Pages 177-88
Authors Hondoh H, Kuriki T, Matsuura Y
Title Three-dimensional structure and substrate binding of Bacillus stearothermophilus neopullulanase.
Related PDB 1j0h 1j0i 1j0j 1j0k
Related UniProtKB P38940
[21]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 15182368
Journal Eur J Biochem
Year 2004
Volume 271
Pages 2530-8
Authors Mizuno M, Tonozuka T, Uechi A, Ohtaki A, Ichikawa K, Kamitori S, Nishikawa A, Sakano Y
Title The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product.
Related PDB 1vb9
Related UniProtKB
[22]
Resource
Comments X-ray crystallography
Medline ID
PubMed ID 15138257
Journal J Biol Chem
Year 2004
Volume 279
Pages 31033-40
Authors Ohtaki A, Mizuno M, Tonozuka T, Sakano Y, Kamitori S
Title Complex structures of Thermoactinomyces vulgaris R-47 alpha-amylase 2 with acarbose and cyclodextrins demonstrate the multiple substrate recognition mechanism.
Related PDB 1vfk 1vfm 1vfo 1vfu
Related UniProtKB

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.

Created Updated
2005-04-21 2009-02-26