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Flavoprotein PDB id
1kif
Jmol
Contents
Protein chains
(+ 2 more) 339 a.a. *
Ligands
FAD ×8
BEZ ×8
Waters ×294
* Residue conservation analysis
PDB id:
1kif
Name: Flavoprotein
Title: D-amino acid oxidase from pig kidney
Structure: D-amino acid oxidase. Chain: a, b, c, d, e, f, g, h. Synonym: daao. Other_details: oxidized state
Source: Sus scrofa. Pig. Organism_taxid: 9823. Organ: kidney. Organelle: peroxisome
Biol. unit: Dimer (from PQS)
Resolution:
2.60Å     R-factor:   0.228     R-free:   0.245
Authors: F.Todone,A.Mattevi
Key ref: A.Mattevi et al. (1996). Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2. Proc Natl Acad Sci U S A, 93, 7496-7501. PubMed id: 8755502 DOI: 10.1073/pnas.93.15.7496
Date:
19-Jan-96     Release date:   11-Jul-96    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P00371  (OXDA_PIG) -  D-amino-acid oxidase
Seq:
Struc: 		347 a.a.
339 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.1.4.3.3  - D-amino-acid oxidase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]

      Pathway: 		Cephalosporin Biosynthesis
      Reaction: A D-amino acid + H2O + O2 = a 2-oxo acid + NH3 + H2O2
D-amino acid
 + H(2)O
 + O(2)
 = 2-oxo acid
 + NH(3)
 + H(2)O(2)
      Cofactor: FAD
FAD
Bound ligand (Het Group name = FAD) corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     peroxisome   1 term 
  Biological process     oxidation-reduction process   2 terms 
  Biochemical function     nucleotide binding     4 terms  

 

 
    reference    
 
 
DOI no: 10.1073/pnas.93.15.7496 Proc Natl Acad Sci U S A 93:7496-7501 (1996)
PubMed id: 8755502  
 
 
Crystal structure of D-amino acid oxidase: a case of active site mirror-image convergent evolution with flavocytochrome b2.
A.Mattevi, M.A.Vanoni, F.Todone, M.Rizzi, A.Teplyakov, A.Coda, M.Bolognesi, B.Curti.
 
  ABSTRACT  
 
D-amino acid oxidase is the prototype of the FAD-dependent oxidases. It catalyses the oxidation of D-amino acids to the corresponding alpha-ketoacids. The reducing equivalents are transferred to molecular oxygen with production of hydrogen peroxide. We have solved the crystal structure of the complex of D-amino acid oxidase with benzoate, a competitive inhibitor of the substrate, by single isomorphous replacement and eightfold averaging. Each monomer is formed by two domains with an overall topology similar to that of p-hydroxybenzoate hydroxylase. The benzoate molecule lays parallel to the flavin ring and is held in position by a salt bridge with Arg-283. Analysis of the active site shows that no side chains are properly positioned to act as the postulated base required for the catalytic carboanion mechanism. On the contrary, the benzoate binding mode suggests a direct transfer of the substrate alpha-hydrogen to the flavin during the enzyme reductive half-reaction.The active site Of D-amino acid oxidase exhibits a striking similarity with that of flavocytochrome b2, a structurally unrelated FMN-dependent flavoenzyme. The active site groups (if these two enzymes are in fact superimposable once the mirror-image of the flavocytochrome b2 active site is generated with respect to the flavin plane. Therefore, the catalytic sites of D-amino acid oxidase and flavocytochrome b2 appear to have converged to a highly similar but enantiomeric architecture in order to catalvze similar reactions (oxidation of alpha-amino acids or alpha-hydroxy acids), although with opposite stereochemistry.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20938508 D.Georgieva, M.Murakami, M.Perband, R.Arni, and C.Betzel (2011).
The structure of a native l-amino acid oxidase, the major component of the Vipera ammodytes ammodytes venomic, reveals dynamic active site and quaternary structure stabilization by divalent ions.
  Mol Biosyst, 7, 379-384.  
21383134 G.Kachalova, K.Decker, A.Holt, and H.D.Bartunik (2011).
Crystallographic snapshots of the complete reaction cycle of nicotine degradation by an amine oxidase of the monoamine oxidase (MAO) family.
  Proc Natl Acad Sci U S A, 108, 4800-4805.  
21458638 H.Zhang, L.Qi, J.Qiao, and L.Mao (2011).
Determination of sodium benzoate by chiral ligand exchange CE based on its inhibitory activity in D-amino acid oxidase mediated oxidation of D-serine.
  Anal Chim Acta, 691, 103-109.  
20567862 M.Katane, Y.Saitoh, K.Maeda, T.Hanai, M.Sekine, T.Furuchi, and H.Homma (2011).
Role of the active site residues arginine-216 and arginine-237 in the substrate specificity of mammalian D-aspartate oxidase.
  Amino Acids, 40, 467-476.  
20195697 L.Pollegioni, and S.Sacchi (2010).
Metabolism of the neuromodulator D-serine.
  Cell Mol Life Sci, 67, 2387-2404.  
20564562 M.Katane, and H.Homma (2010).
D-aspartate oxidase: the sole catabolic enzyme acting on free D-aspartate in mammals.
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20000632 M.S.Adachi, P.R.Juarez, and P.F.Fitzpatrick (2010).
Mechanistic studies of human spermine oxidase: kinetic mechanism and pH effects.
  Biochemistry, 49, 386-392.  
19651103 P.F.Fitzpatrick (2010).
Oxidation of amines by flavoproteins.
  Arch Biochem Biophys, 493, 13-25.  
19132842 M.F.Mora, C.E.Giacomelli, and C.D.Garcia (2009).
Interaction of D-amino acid oxidase with carbon nanotubes: implications in the design of biosensors.
  Anal Chem, 81, 1016-1022.  
18084756 L.Pollegioni, G.Molla, S.Sacchi, E.Rosini, R.Verga, and M.S.Pilone (2008).
Properties and applications of microbial D: -amino acid oxidases: current state and perspectives.
  Appl Microbiol Biotechnol, 78, 1.  
18235994 M.Katane, T.Hanai, T.Furuchi, M.Sekine, and H.Homma (2008).
Hyperactive mutants of mouse D-aspartate oxidase: mutagenesis of the active site residue serine 308.
  Amino Acids, 35, 75-82.  
18156273 S.Grill, S.Busenbender, M.Pfeiffer, U.Köhler, and M.Mack (2008).
The bifunctional flavokinase/flavin adenine dinucleotide synthetase from Streptomyces davawensis produces inactive flavin cofactors and is not involved in resistance to the antibiotic roseoflavin.
  J Bacteriol, 190, 1546-1553.  
17279391 B.Geueke, A.Weckbecker, and W.Hummel (2007).
Overproduction and characterization of a recombinant D-amino acid oxidase from Arthrobacter protophormiae.
  Appl Microbiol Biotechnol, 74, 1240-1247.  
17542620 E.C.Ralph, J.S.Hirschi, M.A.Anderson, W.W.Cleland, D.A.Singleton, and P.F.Fitzpatrick (2007).
Insights into the mechanism of flavoprotein-catalyzed amine oxidation from nitrogen isotope effects on the reaction of N-methyltryptophan oxidase.
  Biochemistry, 46, 7655-7664.  
17469229 M.Katane, T.Furuchi, M.Sekine, and H.Homma (2007).
Molecular cloning of a cDNA encoding mouse D-aspartate oxidase and functional characterization of its recombinant proteins by site-directed mutagenesis.
  Amino Acids, 32, 69-78.  
17140416 M.Katane, Y.Seida, M.Sekine, T.Furuchi, and H.Homma (2007).
Caenorhabditis elegans has two genes encoding functional d-aspartate oxidases.
  FEBS J, 274, 137-149.  
17994768 P.F.Fitzpatrick, D.M.Bozinovski, A.Héroux, P.G.Shaw, M.P.Valley, and A.M.Orville (2007).
Mechanistic and structural analyses of the roles of Arg409 and Asp402 in the reaction of the flavoprotein nitroalkane oxidase.
  Biochemistry, 46, 13800-13808.
PDB codes: 2reh 2zaf
  19890477 P.F.Fitzpatrick (2007).
Insights into the mechanisms of flavoprotein oxidases from kinetic isotope effects.
  J Labelled Comp Radiopharm, 50, 1016-1025.  
16538681 I.Dib, A.Slavica, W.Riethorst, and B.Nidetzky (2006).
Thermal inactivation of D-amino acid oxidase from Trigonopsis variabilis occurs via three parallel paths of irreversible denaturation.
  Biotechnol Bioeng, 94, 645-654.  
16245349 M.Bakke, C.Setoyama, R.Miura, and N.Kajiyama (2006).
Thermostabilization of porcine kidney D-amino acid oxidase by a single amino acid substitution.
  Biotechnol Bioeng, 93, 1023-1027.  
16999821 P.Ferreira, F.J.Ruiz-Dueñas, M.J.Martínez, W.J.van Berkel, and A.T.Martínez (2006).
Site-directed mutagenesis of selected residues at the active site of aryl-alcohol oxidase, an H2O2-producing ligninolytic enzyme.
  FEBS J, 273, 4878-4888.  
17088322 T.Kawazoe, H.Tsuge, M.S.Pilone, and K.Fukui (2006).
Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring.
  Protein Sci, 15, 2708-2717.
PDB code: 2du8
16332786 A.Slavica, I.Dib, and B.Nidetzky (2005).
Single-site oxidation, cysteine 108 to cysteine sulfinic acid, in D-amino acid oxidase from Trigonopsis variabilis and its structural and functional consequences.
  Appl Environ Microbiol, 71, 8061-8068.  
15723552 E.C.Ralph, and P.F.Fitzpatrick (2005).
pH and kinetic isotope effects on sarcosine oxidation by N-methyltryptophan oxidase.
  Biochemistry, 44, 3074-3081.  
15701048 V.I.Tishkov, and S.V.Khoronenkova (2005).
D-Amino acid oxidase: structure, catalytic mechanism, and practical application.
  Biochemistry (Mosc), 70, 40-54.  
15058991 L.Pollegioni, L.Caldinelli, G.Molla, S.Sacchi, and M.S.Pilone (2004).
Catalytic properties of D-amino acid oxidase in cephalosporin C bioconversion: a comparison between proteins from different sources.
  Biotechnol Prog, 20, 467-473.  
15239056 P.F.Mugford, S.M.Lait, B.A.Keay, and R.J.Kazlauskas (2004).
Enantiocomplementary enzymatic resolution of the chiral auxiliary: cis,cis-6-(2,2-dimethylpropanamido)spiro[4.4]nonan-1-ol and the molecular basis for the high enantioselectivity of subtilisin Carlsberg.
  Chembiochem, 5, 980-987.  
15273299 S.Y.Reddy, and T.C.Bruice (2004).
Determination of enzyme mechanisms by molecular dynamics: studies on quinoproteins, methanol dehydrogenase, and soluble glucose dehydrogenase.
  Protein Sci, 13, 1965-1978.  
14596603 A.R.Dewanti, and B.Mitra (2003).
A transient intermediate in the reaction catalyzed by (S)-mandelate dehydrogenase from Pseudomonas putida.
  Biochemistry, 42, 12893-12901.  
12654003 G.Molla, L.Motteran, V.Job, M.S.Pilone, and L.Pollegioni (2003).
Kinetic mechanisms of glycine oxidase from Bacillus subtilis.
  Eur J Biochem, 270, 1474-1482.  
12596267 T.Hamelryck (2003).
Efficient identification of side-chain patterns using a multidimensional index tree.
  Proteins, 51, 96.  
12514740 Y.H.Lee, S.Nadaraia, D.Gu, D.F.Becker, and J.J.Tanner (2003).
Structure of the proline dehydrogenase domain of the multifunctional PutA flavoprotein.
  Nat Struct Biol, 10, 109-114.
PDB code: 1k87
12354107 A.Boselli, S.Sacchi, V.Job, M.S.Pilone, and L.Pollegioni (2002).
Role of tyrosine 238 in the active site of Rhodotorula gracilis D-amino acid oxidase. A site-directed mutagenesis study.
  Eur J Biochem, 269, 4762-4771.  
12146940 G.Zhao, and M.S.Jorns (2002).
Monomeric sarcosine oxidase: evidence for an ionizable group in the E.S complex.
  Biochemistry, 41, 9747-9750.  
11861643 R.M.Geha, K.Chen, J.Wouters, F.Ooms, and J.C.Shih (2002).
Analysis of conserved active site residues in monoamine oxidase A and B and their three-dimensional molecular modeling.
  J Biol Chem, 277, 17209-17216.  
11874460 V.Job, G.Molla, M.S.Pilone, and L.Pollegioni (2002).
Overexpression of a recombinant wild-type and His-tagged Bacillus subtilis glycine oxidase in Escherichia coli.
  Eur J Biochem, 269, 1456-1463.  
  11377202 C.Breithaupt, J.Strassner, U.Breitinger, R.Huber, P.Macheroux, A.Schaller, and T.Clausen (2001).
X-ray structure of 12-oxophytodienoate reductase 1 provides structural insight into substrate binding and specificity within the family of OYE.
  Structure, 9, 419-429.
PDB codes: 1icp 1icq 1ics
11683874 C.M.Harris, L.Pollegioni, and S.Ghisla (2001).
pH and kinetic isotope effects in d-amino acid oxidase catalysis.
  Eur J Biochem, 268, 5504-5520.  
11559361 M.Gondry, J.Dubois, M.Terrier, and F.Lederer (2001).
The catalytic role of tyrosine 254 in flavocytochrome b2 (L-lactate dehydrogenase from baker's yeast). Comparison between the Y254F and Y254L mutant proteins.
  Eur J Biochem, 268, 4918-4927.  
11895118 R.Miura (2001).
Versatility and specificity in flavoenzymes: control mechanisms of flavin reactivity.
  Chem Rec, 1, 183-194.  
11157233 Y.Liu, T.M.Louie, J.Payne, J.Bohuslavek, H.Bolton, and L.Xun (2001).
Identification, purification, and characterization of iminodiacetate oxidase from the EDTA-degrading bacterium BNC1.
  Appl Environ Microbiol, 67, 696-701.  
11761335 Y.Yano (2001).
Artificial flavin receptors: effects of hydrogen bonding on redox properties of a flavin mimic.
  Antioxid Redox Signal, 3, 899-909.  
10716694 A.A.Raibekas, K.Fukui, and V.Massey (2000).
Design and properties of human D-amino acid oxidase with covalently attached flavin.
  Proc Natl Acad Sci U S A, 97, 3089-3093.  
10962107 E.Varela, M.Jesús Martínez, and A.T.Martínez (2000).
Aryl-alcohol oxidase protein sequence: a comparison with glucose oxidase and other FAD oxidoreductases.
  Biochim Biophys Acta, 1481, 202-208.
PDB code: 1qjn
10653664 G.Gadda, A.Banerjee, and P.F.Fitzpatrick (2000).
Identification of an essential tyrosine residue in nitroalkane oxidase by modification with tetranitromethane.
  Biochemistry, 39, 1162-1168.  
10684621 G.Gadda, and P.F.Fitzpatrick (2000).
Mechanism of nitroalkane oxidase: 2. pH and kinetic isotope effects.
  Biochemistry, 39, 1406-1410.  
11087383 G.Zhao, J.Qu, F.A.Davis, and M.S.Jorns (2000).
Inactivation of monomeric sarcosine oxidase by reaction with N-(cyclopropyl)glycine.
  Biochemistry, 39, 14341-14347.  
10706608 K.Yorita, H.Misaki, B.A.Palfey, and V.Massey (2000).
On the interpretation of quantitative structure-function activity relationship data for lactate oxidase.
  Proc Natl Acad Sci U S A, 97, 2480-2485.  
10978770 L.Lin, H.R.Chien, W.Wang, T.Hwang, H.Fu, and W.Hsu (2000).
Expression of Trigonopsis variabilis D-amino acid oxidase gene in Escherichia coli and characterization of its inactive mutants.
  Enzyme Microb Technol, 27, 482-491.  
11054115 L.Pollegioni, D.Porrini, G.Molla, and M.S.Pilone (2000).
Redox potentials and their pH dependence of D-amino-acid oxidase of Rhodotorula gracilis and Trigonopsis variabilis.
  Eur J Biochem, 267, 6624-6632.  
10944103 P.D.Pawelek, J.Cheah, R.Coulombe, P.Macheroux, S.Ghisla, and A.Vrielink (2000).
The structure of L-amino acid oxidase reveals the substrate trajectory into an enantiomerically conserved active site.
  EMBO J, 19, 4204-4215.
PDB codes: 1f8r 1f8s
10684595 R.J.Harris, R.Meskys, M.J.Sutcliffe, and N.S.Scrutton (2000).
Kinetic studies of the mechanism of carbon-hydrogen bond breakage by the heterotetrameric sarcosine oxidase of Arthrobacter sp. 1-IN.
  Biochemistry, 39, 1189-1198.  
11070076 S.Umhau, L.Pollegioni, G.Molla, K.Diederichs, W.Welte, M.S.Pilone, and S.Ghisla (2000).
The x-ray structure of D-amino acid oxidase at very high resolution identifies the chemical mechanism of flavin-dependent substrate dehydrogenation.
  Proc Natl Acad Sci U S A, 97, 12463-12468.
PDB codes: 1c0k 1c0l 1c0p
10508675 A.E.Todd, C.A.Orengo, and J.M.Thornton (1999).
Evolution of protein function, from a structural perspective.
  Curr Opin Chem Biol, 3, 548-556.  
  10425677 A.Mattevi, G.Tedeschi, L.Bacchella, A.Coda, A.Negri, and S.Ronchi (1999).
Structure of L-aspartate oxidase: implications for the succinate dehydrogenase/fumarate reductase oxidoreductase family.
  Structure, 7, 745-756.
PDB code: 1chu
10508152 A.Oubrie, H.J.Rozeboom, K.H.Kalk, A.J.Olsthoorn, J.A.Duine, and B.W.Dijkstra (1999).
Structure and mechanism of soluble quinoprotein glucose dehydrogenase.
  EMBO J, 18, 5187-5194.
PDB codes: 1c9u 1cq1
  10368296 C.Binda, A.Coda, R.Angelini, R.Federico, P.Ascenzi, and A.Mattevi (1999).
A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase.
  Structure, 7, 265-276.
PDB codes: 1b37 1b5q
10231533 G.Gadda, L.J.Dangott, W.H.Johnson, C.P.Whitman, and P.F.Fitzpatrick (1999).
Characterization of 2-oxo-3-pentynoate as an active-site-directed inactivator of flavoprotein oxidases: identification of active-site peptides in tryptophan 2-monooxygenase.
  Biochemistry, 38, 5822-5828.  
10103021 G.Tedeschi, A.Negri, F.Ceciliani, A.Mattevi, and S.Ronchi (1999).
Structural characterization of l-aspartate oxidase and identification of an interdomain loop by limited proteolysis.
  Eur J Biochem, 260, 896-903.  
10231535 I.E.Lehoux, and B.Mitra (1999).
(S)-Mandelate dehydrogenase from Pseudomonas putida: mechanistic studies with alternate substrates and pH and kinetic isotope effects.
  Biochemistry, 38, 5836-5848.  
10089375 L.Bacchella, C.Lina, F.Todone, A.Negri, G.Tedeschi, S.Ronchi, and A.Mattevi (1999).
Crystallization of L-aspartate oxidase, the first enzyme in the bacterial de novo biosynthesis of NAD.
  Acta Crystallogr D Biol Crystallogr, 55, 549-551.  
  10427728 L.L.Lin, W.C.Wang, S.S.Ju, H.R.Chien, and W.H.Hsu (1999).
The role of a conserved histidine residue, His324, in Trigonopsis variabilis D-amino acid oxidase.
  FEMS Microbiol Lett, 176, 443-448.  
  10427080 M.Gabler, and L.Fischer (1999).
Production of a new D-amino acid oxidase from the fungus Fusarium oxysporum.
  Appl Environ Microbiol, 65, 3750-3753.  
  10569769 O.Cohavy, G.Harth, M.Horwitz, M.Eggena, C.Landers, C.Sutton, S.R.Targan, and J.Braun (1999).
Identification of a novel mycobacterial histone H1 homologue (HupB) as an antigenic target of pANCA monoclonal antibody and serum immunoglobulin A from patients with Crohn's disease.
  Infect Immun, 67, 6510-6517.  
  10368302 P.Trickey, M.A.Wagner, M.S.Jorns, and F.S.Mathews (1999).
Monomeric sarcosine oxidase: structure of a covalently flavinylated amine oxidizing enzyme.
  Structure, 7, 331-345.
PDB codes: 1b3m 1l9f 2gb0
9546198 A.Mattevi (1998).
The PHBH fold: not only flavoenzymes.
  Biophys Chem, 70, 217-222.  
  9634698 C.Enroth, H.Neujahr, G.Schneider, and Y.Lindqvist (1998).
The crystal structure of phenol hydroxylase in complex with FAD and phenol provides evidence for a concerted conformational change in the enzyme and its cofactor during catalysis.
  Structure, 6, 605-617.
PDB code: 1foh
9558355 G.Gadda, and P.F.Fitzpatrick (1998).
Biochemical and physical characterization of the active FAD-containing form of nitroalkane oxidase from Fusarium oxysporum.
  Biochemistry, 37, 6154-6164.  
9772189 G.J.Mancini-Samuelson, V.Kieweg, K.M.Sabaj, S.Ghisla, and M.T.Stankovich (1998).
Redox properties of human medium-chain acyl-CoA dehydrogenase, modulation by charged active-site amino acid residues.
  Biochemistry, 37, 14605-14612.  
  9684885 K.S.Rao, and F.Lederer (1998).
About the pKa of the active-site histidine in flavocytochrome b2 (yeast L-lactate dehydrogenase).
  Protein Sci, 7, 1531-1537.  
9434899 A.Mattevi, M.A.Vanoni, and B.Curti (1997).
Structure of D-amino acid oxidase: new insights from an old enzyme.
  Curr Opin Struct Biol, 7, 804-810.  
9141139 A.Mattevi, M.W.Fraaije, A.Coda, and W.J.van Berkel (1997).
Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum.
  Proteins, 27, 601-603.
PDB codes: 1ahu 1ahv 1ahz 1vao 2vao
  9261083 A.Mattevi, M.W.Fraaije, A.Mozzarelli, L.Olivi, A.Coda, and W.J.van Berkel (1997).
Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity.
  Structure, 5, 907-920.
PDB codes: 1ahu 1ahv 1ahz 1vao 2vao
9434346 F.J.González, J.Montes, F.Martin, M.C.López, E.Fermiñán, J.Catalán, M.A.Galán, and A.Domínguez (1997).
Molecular cloning of TvDAO1, a gene encoding a D-amino acid oxidase from Trigonopsis variabilis and its expression in Saccharomyces cerevisiae and Kluyveromyces lactis.
  Yeast, 13, 1399-1408.  
9153426 F.Todone, M.A.Vanoni, A.Mozzarelli, M.Bolognesi, A.Coda, B.Curti, and A.Mattevi (1997).
Active site plasticity in D-amino acid oxidase: a crystallographic analysis.
  Biochemistry, 36, 5853-5860.
PDB codes: 1dao 1ddo
  9371431 J.Miranda-Ríos, C.Morera, H.Taboada, A.Dávalos, S.Encarnación, J.Mora, and M.Soberón (1997).
Expression of thiamin biosynthetic genes (thiCOGE) and production of symbiotic terminal oxidase cbb3 in Rhizobium etli.
  J Bacteriol, 179, 6887-6893.  
9275167 K.Yorita, K.Janko, K.Aki, S.Ghisla, B.A.Palfey, and V.Massey (1997).
On the reaction mechanism of L-lactate oxidase: quantitative structure-activity analysis of the reaction with para-substituted L-mandelates.
  Proc Natl Acad Sci U S A, 94, 9590-9595.  
9153402 M.A.Vanoni, A.Cosma, D.Mazzeo, A.Mattevi, F.Todone, and B.Curti (1997).
Limited proteolysis and X-ray crystallography reveal the origin of substrate specificity and of the rate-limiting product release during oxidation of D-amino acids catalyzed by mammalian D-amino acid oxidase.
  Biochemistry, 36, 5624-5632.  
8841131 W.C.Alston, M.Kanska, and C.J.Murray (1996).
Secondary H/T and D/T isotope effects in enzymatic enolization reactions. Coupled motion and tunneling in the triosephosphate isomerase reaction.
  Biochemistry, 35, 12873-12881.  
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 codes are shown on the right.