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Transferase(glucanotransferase) PDB id
1cdg
Jmol
Contents
Protein chain
686 a.a. *
Ligands
MAL ×3
Metals
_CA ×2
Waters ×471
* Residue conservation analysis
PDB id:
1cdg
Name: Transferase(glucanotransferase)
Title: Nucleotide sequence and x-ray structure of cyclodextrin glycosyltransferase from bacillus circulans strain 251 in a maltose-dependent crystal form
Structure: Cyclodextrin glycosyl-transferase. Chain: a. Engineered: yes
Source: Bacillus circulans. Organism_taxid: 1397
Resolution:
2.00Å     R-factor:   0.164    
Authors: C.L.Lawson,R.Van Montfort,B.V.Strokopytov,K.H.Kalk, H.J.Rozeboom,B.W.Dijkstra
Key ref: C.L.Lawson et al. (1994). Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form. J Mol Biol, 236, 590-600. PubMed id: 8107143 DOI: 10.1006/jmbi.1994.1168
Date:
02-Aug-93     Release date:   31-Jan-94    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P43379  (CDGT2_BACCI) -  Cyclomaltodextrin glucanotransferase
Seq:
Struc: 		 
Seq:
Struc: 		713 a.a.
686 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.2.4.1.19  - Cyclomaltodextrin glucanotransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Degrades starch to cyclodextrins by formation of a 1,4-alpha-D- glucosidic bond.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   1 term 
  Biological process     carbohydrate metabolic process   1 term 
  Biochemical function     catalytic activity     9 terms  

 

 
DOI no: 10.1006/jmbi.1994.1168 J Mol Biol 236:590-600 (1994)
PubMed id: 8107143  
 
 
Nucleotide sequence and X-ray structure of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 in a maltose-dependent crystal form.
C.L.Lawson, R.van Montfort, B.Strokopytov, H.J.Rozeboom, K.H.Kalk, G.E.de Vries, D.Penninga, L.Dijkhuizen, B.W.Dijkstra.
 
  ABSTRACT  
 
The cyclodextrin glycosyltransferase (CGTase, EC 2.4.1.19) gene from Bacillus circulans strain 251 was cloned and sequenced. It was found to code for a mature protein of 686 amino acid residues, showing 75% identity to the CGTase from B. circulans strain 8. The X-ray structure of the CGTase was elucidated in a maltodextrin-dependent crystal form and refined against X-ray diffraction data to 2.0 A resolution. The structure of the enzyme is nearly identical to the CGTase from B. circulans strain 8. Three maltose binding sites are observed at the protein surface, two in domain E and one in domain C. The maltose-dependence of CGTase crystallization can be ascribed to the proximity of two of the maltose binding sites to intermolecular crystal contacts. The maltose molecules bound in the E domain interact with several residues implicated in a raw starch binding motif conserved among a diverse group of starch converting enzymes.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19763564 H.Leemhuis, R.M.Kelly, and L.Dijkhuizen (2010).
Engineering of cyclodextrin glucanotransferases and the impact for biotechnological applications.
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The carbohydrate-binding module family 20--diversity, structure, and function.
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19139240 M.Palomo, S.Kralj, M.J.van der Maarel, and L.Dijkhuizen (2009).
The unique branching patterns of Deinococcus glycogen branching enzymes are determined by their N-terminal domains.
  Appl Environ Microbiol, 75, 1355-1362.  
19367403 R.M.Kelly, L.Dijkhuizen, and H.Leemhuis (2009).
The evolution of cyclodextrin glucanotransferase product specificity.
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18246304 R.E.Vollú, F.F.da Mota, E.A.Gomes, and L.Seldin (2008).
Cyclodextrin production and genetic characterization of cyclodextrin glucanotranferase of Paenibacillus graminis.
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18726621 R.M.Ong, K.M.Goh, N.M.Mahadi, O.Hassan, R.N.Rahman, and R.M.Illias (2008).
Cloning, extracellular expression and characterization of a predominant beta-CGTase from Bacillus sp. G1 in E. coli.
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Fusion proteins comprising the catalytic domain of mutansucrase and a starch-binding domain can alter the morphology of amylose-free potato starch granules during biosynthesis.
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17207263 F.Nazarian Firouzabadi, J.P.Vincken, Q.Ji, L.C.Suurs, and R.G.Visser (2007).
Expression of an engineered granule-bound Escherichia coli maltose acetyltransferase in wild-type and amf potato plants.
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17891389 Z.Li, M.Wang, F.Wang, Z.Gu, G.Du, J.Wu, and J.Chen (2007).
gamma-Cyclodextrin: a review on enzymatic production and applications.
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16012834 K.Hirano, T.Ishihara, S.Ogasawara, H.Maeda, K.Abe, T.Nakajima, and Y.Yamagata (2006).
Molecular cloning and characterization of a novel gamma-CGTase from alkalophilic Bacillus sp.
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16461650 K.Mukai, H.Watanabe, M.Kubota, H.Chaen, S.Fukuda, and M.Kurimoto (2006).
Purification, characterization, and gene cloning of a novel maltosyltransferase from an Arthrobacter globiformis strain that produces an alternating alpha-1,4- and alpha-1,6-cyclic tetrasaccharide from starch.
  Appl Environ Microbiol, 72, 1065-1071.  
16703471 L.L.Lin, P.J.Chen, J.S.Liu, W.C.Wang, and H.F.Lo (2006).
Identification of glutamate residues important for catalytic activity or thermostability of a truncated Bacillus sp. strain TS-23 alpha-amylase by site-directed mutagenesis.
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16862594 N.Palopoli, M.V.Busi, M.S.Fornasari, D.Gomez-Casati, R.Ugalde, and G.Parisi (2006).
Starch-synthase III family encodes a tandem of three starch-binding domains.
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16517633 Z.Wang, Q.Qi, and P.G.Wang (2006).
Engineering of cyclodextrin glucanotransferase on the cell surface of Saccharomyces cerevisiae for improved cyclodextrin production.
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16041515 H.B.Huang, M.C.Chi, W.H.Hsu, W.C.Liang, and L.L.Lin (2005).
Construction and one-step purification of Bacillus kaustophilus leucine aminopeptidase fused to the starch-binding domain of Bacillus sp. strain TS-23 alpha-amylase.
  Bioprocess Biosyst Eng, 27, 389-398.  
  16508106 K.Imamura, T.Matsuura, Z.Ye, T.Takaha, K.Fujii, M.Kusunoki, and Y.Nitta (2005).
Crystallization and preliminary X-ray crystallographic study of disproportionating enzyme from potato.
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16262690 M.Machovic, B.Svensson, E.A.MacGregor, and S.Janecek (2005).
A new clan of CBM families based on bioinformatics of starch-binding domains from families CBM20 and CBM21.
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15630515 Q.Qi, and W.Zimmermann (2005).
Cyclodextrin glucanotransferase: from gene to applications.
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15939348 R.Rodríguez-Sanoja, N.Oviedo, and S.Sánchez (2005).
Microbial starch-binding domain.
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14705029 H.Leemhuis, H.J.Rozeboom, B.W.Dijkstra, and L.Dijkhuizen (2004).
Improved thermostability of bacillus circulans cyclodextrin glycosyltransferase by the introduction of a salt bridge.
  Proteins, 54, 128-134.
PDB code: 1pj9
15182368 M.Mizuno, T.Tonozuka, A.Uechi, A.Ohtaki, K.Ichikawa, S.Kamitori, A.Nishikawa, and Y.Sakano (2004).
The crystal structure of Thermoactinomyces vulgaris R-47 alpha-amylase II (TVA II) complexed with transglycosylated product.
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PDB code: 1vb9
17147616 Q.Ji, R.J.Oomen, J.P.Vincken, D.N.Bolam, H.J.Gilbert, L.C.Suurs, and R.G.Visser (2004).
Reduction of starch granule size by expression of an engineered tandem starch-binding domain in potato plants.
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12747837 G.Polekhina, A.Gupta, B.J.Michell, B.van Denderen, S.Murthy, S.C.Feil, I.G.Jennings, D.J.Campbell, L.A.Witters, M.W.Parker, B.E.Kemp, and D.Stapleton (2003).
AMPK beta subunit targets metabolic stress sensing to glycogen.
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12492486 H.Leemhuis, B.W.Dijkstra, and L.Dijkhuizen (2003).
Thermoanaerobacterium thermosulfurigenes cyclodextrin glycosyltransferase.
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12554949 H.W.Choe, K.S.Park, J.Labahn, J.Granzin, C.J.Kim, and G.Büldt (2003).
Crystallization and preliminary X-ray diffraction studies of alpha-cyclodextrin glucanotransferase isolated from Bacillus macerans.
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12581203 S.Janecek, B.Svensson, and E.A.MacGregor (2003).
Relation between domain evolution, specificity, and taxonomy of the alpha-amylase family members containing a C-terminal starch-binding domain.
  Eur J Biochem, 270, 635-645.  
11790748 N.Rashid, J.Cornista, S.Ezaki, T.Fukui, H.Atomi, and T.Imanaka (2002).
Characterization of an archaeal cyclodextrin glucanotransferase with a novel C-terminal domain.
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11703654 A.V.Kajava, N.Cheng, R.Cleaver, M.Kessel, M.N.Simon, E.Willery, F.Jacob-Dubuisson, C.Locht, and A.C.Steven (2001).
Beta-helix model for the filamentous haemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins.
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11257505 E.A.MacGregor, S.Janecek, and B.Svensson (2001).
Relationship of sequence and structure to specificity in the alpha-amylase family of enzymes.
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11443082 M.Hemker, A.Stratmann, K.Goeke, W.Schröder, J.Lenz, W.Piepersberg, and H.Pape (2001).
Identification, cloning, expression, and characterization of the extracellular acarbose-modifying glycosyltransferase, AcbD, from Actinoplanes sp. strain SE50.
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11302176 T.Yokota, T.Tonozuka, S.Kamitori, and Y.Sakano (2001).
The deletion of amino-terminal domain in Thermoactinomyces vulgaris R-47 alpha-amylases: effects of domain N on activity, specificity, stability and dimerization.
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11282590 Y.Terada, H.Sanbe, T.Takaha, S.Kitahata, K.Koizumi, and S.Okada (2001).
Comparative study of the cyclization reactions of three bacterial cyclomaltodextrin glucanotransferases.
  Appl Environ Microbiol, 67, 1453-1460.  
11064053 A.D.Blackwood, and C.Bucke (2000).
Addition of polar organic solvents can improve the product selectivity of cyclodextrin glycosyltransferase. Solvent effects on cgtase.
  Enzyme Microb Technol, 27, 704-708.  
10651801 B.A.van der Veen, G.J.van Alebeek, J.C.Uitdehaag, B.W.Dijkstra, and L.Dijkhuizen (2000).
The three transglycosylation reactions catalyzed by cyclodextrin glycosyltransferase from Bacillus circulans (strain 251) proceed via different kinetic mechanisms.
  Eur J Biochem, 267, 658-665.  
10848958 B.A.van der Veen, J.C.Uitdehaag, B.W.Dijkstra, and L.Dijkhuizen (2000).
The role of arginine 47 in the cyclization and coupling reactions of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 implications for product inhibition and product specificity.
  Eur J Biochem, 267, 3432-3441.  
10985769 G.Parsiegla, C.Reverbel-Leroy, C.Tardif, J.P.Belaich, H.Driguez, and R.Haser (2000).
Crystal structures of the cellulase Cel48F in complex with inhibitors and substrates give insights into its processive action.
  Biochemistry, 39, 11238-11246.
PDB codes: 1f9d 1f9o 1fae 1fbo 1fbw
10869182 J.C.Uitdehaag, G.J.van Alebeek, B.A.van Der Veen, L.Dijkhuizen, and B.W.Dijkstra (2000).
Structures of maltohexaose and maltoheptaose bound at the donor sites of cyclodextrin glycosyltransferase give insight into the mechanisms of transglycosylation activity and cyclodextrin size specificity.
  Biochemistry, 39, 7772-7780.
PDB codes: 1eo5 1eo7
10877806 K.Ohdan, T.Kuriki, H.Takata, H.Kaneko, and S.Okada (2000).
Introduction of raw starch-binding domains into Bacillus subtilis alpha-amylase by fusion with the starch-binding domain of Bacillus cyclomaltodextrin glucanotransferase.
  Appl Environ Microbiol, 66, 3058-3064.  
10793202 L.M.Hamilton, C.T.Kelly, and W.M.Fogarty (2000).
Review: cyclodextrins and their interaction with amylolytic enzymes.
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10705452 N.Ichikawa, R.Fujisaka, and R.Kuribayashi (2000).
Requirement for lysine-19 of the yeast mitochondrial ATPase inhibitor for the stability of the inactivated inhibitor-F1Fo complex at higher pH.
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10679895 N.Ishii, K.Haga, K.Yamane, and K.Harata (2000).
Crystal structure of asparagine 233-replaced cyclodextrin glucanotransferase from alkalophilic Bacillus sp. 1011 determined at 1.9 A resolution.
  J Mol Recognit, 13, 35-43.
PDB code: 1d7f
10353816 B.Mikami, M.Adachi, T.Kage, E.Sarikaya, T.Nanmori, R.Shinke, and S.Utsumi (1999).
Structure of raw starch-digesting Bacillus cereus beta-amylase complexed with maltose.
  Biochemistry, 38, 7050-7061.
PDB codes: 1b90 1b9z
  10210191 D.H.Juers, R.E.Huber, and B.W.Matthews (1999).
Structural comparisons of TIM barrel proteins suggest functional and evolutionary relationships between beta-galactosidase and other glycohydrolases.
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10393270 G.T.Robillard, and J.Broos (1999).
Structure/function studies on the bacterial carbohydrate transporters, enzymes II, of the phosphoenolpyruvate-dependent phosphotransferase system.
  Biochim Biophys Acta, 1422, 73.  
10574960 J.C.Uitdehaag, K.H.Kalk, B.A.van Der Veen, L.Dijkhuizen, and B.W.Dijkstra (1999).
The cyclization mechanism of cyclodextrin glycosyltransferase (CGTase) as revealed by a gamma-cyclodextrin-CGTase complex at 1.8-A resolution.
  J Biol Chem, 274, 34868-34876.
PDB code: 1d3c
  10049841 Y.Terada, K.Fujii, T.Takaha, and S.Okada (1999).
Thermus aquaticus ATCC 33923 amylomaltase gene cloning and expression and enzyme characterization: production of cycloamylose.
  Appl Environ Microbiol, 65, 910-915.  
10387084 Z.Dauter, M.Dauter, A.M.Brzozowski, S.Christensen, T.V.Borchert, L.Beier, K.S.Wilson, and G.J.Davies (1999).
X-ray structure of Novamyl, the five-domain "maltogenic" alpha-amylase from Bacillus stearothermophilus: maltose and acarbose complexes at 1.7A resolution.
  Biochemistry, 38, 8385-8392.
PDB codes: 1qho 1qhp
9558324 A.K.Schmidt, S.Cottaz, H.Driguez, and G.E.Schulz (1998).
Structure of cyclodextrin glycosyltransferase complexed with a derivative of its main product beta-cyclodextrin.
  Biochemistry, 37, 5909-5915.
PDB code: 3cgt
9671514 B.W.Sigurskjold, T.Christensen, N.Payre, S.Cottaz, H.Driguez, and B.Svensson (1998).
Thermodynamics of binding of heterobidentate ligands consisting of spacer-connected acarbose and beta-cyclodextrin to the catalytic and starch-binding domains of glucoamylase from Aspergillus niger shows that the catalytic and starch-binding sites are in close proximity in space.
  Biochemistry, 37, 10446-10452.  
9488711 R.D.Wind, J.C.Uitdehaag, R.M.Buitelaar, B.W.Dijkstra, and L.Dijkhuizen (1998).
Engineering of cyclodextrin product specificity and pH optima of the thermostable cyclodextrin glycosyltransferase from Thermoanaerobacterium thermosulfurigenes EM1.
  J Biol Chem, 273, 5771-5779.
PDB code: 1a47
  9385633 A.C.Wallace, N.Borkakoti, and J.M.Thornton (1997).
TESS: a geometric hashing algorithm for deriving 3D coordinate templates for searching structural databases. Application to enzyme active sites.
  Protein Sci, 6, 2308-2323.  
  9416598 K.S.Devulapalle, S.D.Goodman, Q.Gao, A.Hemsley, and G.Mooser (1997).
Knowledge-based model of a glucosyltransferase from the oral bacterial group of mutans streptococci.
  Protein Sci, 6, 2489-2493.  
  9195884 K.Sorimachi, M.F.Le Gal-Coëffet, G.Williamson, D.B.Archer, and M.P.Williamson (1997).
Solution structure of the granular starch binding domain of Aspergillus niger glucoamylase bound to beta-cyclodextrin.
  Structure, 5, 647-661.
PDB codes: 1ac0 1acz
9200704 M.P.Williamson, M.F.Le Gal-Coëffet, K.Sorimachi, C.S.Furniss, D.B.Archer, and G.Williamson (1997).
Function of conserved tryptophans in the Aspergillus niger glucoamylase 1 starch binding domain.
  Biochemistry, 36, 7535-7539.  
9365988 P.M.Coutinho, and P.J.Reilly (1997).
Glucoamylase structural, functional, and evolutionary relationships.
  Proteins, 29, 334-347.  
  9032081 R.L.van Montfort, T.Pijning, K.H.Kalk, J.Reizer, M.H.Saier, M.M.Thunnissen, G.T.Robillard, and B.W.Dijkstra (1997).
The structure of an energy-coupling protein from bacteria, IIBcellobiose, reveals similarity to eukaryotic protein tyrosine phosphatases.
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PDB code: 1iib
9245426 R.Mosi, S.He, J.Uitdehaag, B.W.Dijkstra, and S.G.Withers (1997).
Trapping and characterization of the reaction intermediate in cyclodextrin glycosyltransferase by use of activated substrates and a mutant enzyme.
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8672460 B.Strokopytov, R.M.Knegtel, D.Penninga, H.J.Rozeboom, K.H.Kalk, L.Dijkhuizen, and B.W.Dijkstra (1996).
Structure of cyclodextrin glycosyltransferase complexed with a maltononaose inhibitor at 2.6 angstrom resolution. Implications for product specificity.
  Biochemistry, 35, 4241-4249.
PDB codes: 1dij 2dij
8955113 D.Penninga, B.A.van der Veen, R.M.Knegtel, S.A.van Hijum, H.J.Rozeboom, K.H.Kalk, B.W.Dijkstra, and L.Dijkhuizen (1996).
The raw starch binding domain of cyclodextrin glycosyltransferase from Bacillus circulans strain 251.
  J Biol Chem, 271, 32777-32784.
PDB code: 1tcm
8718854 J.Sakon, W.S.Adney, M.E.Himmel, S.R.Thomas, and P.A.Karplus (1996).
Crystal structure of thermostable family 5 endocellulase E1 from Acidothermus cellulolyticus in complex with cellotetraose.
  Biochemistry, 35, 10648-10660.
PDB code: 1ece
  8762144 S.Janecek (1996).
Invariant glycines and prolines flanking in loops the strand beta 2 of various (alpha/beta)8-barrel enzymes: a hidden homology?
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7588803 A.J.Jacks, K.Sorimachi, M.F.Le Gal-Coëffet, G.Williamson, D.B.Archer, and M.P.Williamson (1995).
1H and 15N assignments and secondary structure of the starch-binding domain of glucoamylase from Aspergillus niger.
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18623437 B.K.Dalmia, K.Schütte, and Z.L.Nikolov (1995).
Domain E of Bacillus macerans cyclodextrin glucanotransferase: An independent starch-binding domain.
  Biotechnol Bioeng, 47, 575-584.  
7588802 M.F.Le Gal-Coëffet, A.J.Jacks, K.Sorimachi, M.P.Williamson, G.Williamson, and D.B.Archer (1995).
Expression in Aspergillus niger of the starch-binding domain of glucoamylase. Comparison with the proteolytically produced starch-binding domain.
  Eur J Biochem, 233, 561-567.  
  7613472 M.Qian, R.Haser, and F.Payan (1995).
Carbohydrate binding sites in a pancreatic alpha-amylase-substrate complex, derived from X-ray structure analysis at 2.1 A resolution.
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  7747949 R.D.Wind, W.Liebl, R.M.Buitelaar, D.Penninga, A.Spreinat, L.Dijkhuizen, and H.Bahl (1995).
Cyclodextrin formation by the thermostable alpha-amylase of Thermoanaerobacterium thermosulfurigenes EM1 and reclassification of the enzyme as a cyclodextrin glycosyltransferase.
  Appl Environ Microbiol, 61, 1257-1265.  
7493956 R.M.Knegtel, B.Strokopytov, D.Penninga, O.G.Faber, H.J.Rozeboom, K.H.Kalk, L.Dijkhuizen, and B.W.Dijkstra (1995).
Crystallographic studies of the interaction of cyclodextrin glycosyltransferase from Bacillus circulans strain 251 with natural substrates and products.
  J Biol Chem, 270, 29256-29264.
PDB codes: 1cxe 1cxf 1cxh 1cxi
  7549888 S.Janecek (1995).
Similarity of different beta-strands flanked in loops by glycines and prolines from distinct (alpha/beta)8-barrel enzymes: chance or a homology?
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  7704528 A.C.Terwisscha van Scheltinga, K.H.Kalk, J.J.Beintema, and B.W.Dijkstra (1994).
Crystal structures of hevamine, a plant defence protein with chitinase and lysozyme activity, and its complex with an inhibitor.
  Structure, 2, 1181-1189.
PDB codes: 1hvm 1hvq
7813489 B.Schwermann, K.Pfau, B.Liliensiek, M.Schleyer, T.Fischer, and E.P.Bakker (1994).
Purification, properties and structural aspects of a thermoacidophilic alpha-amylase from Alicyclobacillus acidocaldarius atcc 27009. Insight into acidostability of proteins.
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7712292 J.D.McCarter, and S.G.Withers (1994).
Mechanisms of enzymatic glycoside hydrolysis.
  Curr Opin Struct Biol, 4, 885-892.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.