The manifold of vitamin B6 dependent enzymes

Structure

Volumn 8, Issue 1, 2000, Pages

  Schneider, Gunter ^a   Käck, Helena ^a   Lindqvist, Ylva ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE RACEMASE; ASPARTATE AMINOTRANSFERASE; ENZYME; GLYCOGEN PHOSPHORYLASE; PYRIDOXINE; TRYPTOPHAN SYNTHASE; ALANINE AMINOTRANSFERASE; DEXTRO AMINO ACID AMINOTRANSFERASE; PHOSPHORYLASE;

CHEMICAL REACTION; ENZYME STRUCTURE; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FOLDING; SHORT SURVEY; STRUCTURE ANALYSIS; ANIMAL; CHEMISTRY; HUMAN; METABOLISM; PROTEIN SECONDARY STRUCTURE; PROTEIN TERTIARY STRUCTURE; REVIEW;

ALANINE RACEMASE; ALANINE TRANSAMINASE; ANIMALS; ASPARTATE AMINOTRANSFERASES; D-ALANINE TRANSAMINASE; ENZYMES; HUMANS; PHOSPHORYLASES; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PYRIDOXINE; TRYPTOPHAN SYNTHASE;

EID: 0343851637     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)00085-X     Document Type: Review

References (52)

1. Braunstein A.E., Shemyakin M.M. The theory of processes of amino acid metabolism catalysed by pyridoxal 5′-phosphate-dependent enzymes. Biokhimia. 18:1953;393-411.
2. 6-catalysed reactions. J. Am. Chem. Soc. 76:1953;648-652.
3. John R.A. Pyridoxal phosphate-dependent enzymes. Biochim. Biophys. Acta. 1248:1995;81-96.
4. Hayashi H. Pyridoxal enzymes: mechanistic diversity and uniformity. J. Biochem. 118:1995;463-473.
5. Yoshimura T., Jhee K.-H., Soda K. Stereospecificity for the hydrogen transfer and molecular evolution of pyridoxal enzymes. Biosci. Biotech. Biochem. 60:1996;181-187.
6. 6-dependent enzymes. Curr. Opin. Struct. Biol. 8:1998;759-769.
7. Dunathan H.C. Conformation and reaction specificity in pyridoxal phosphate enzymes. Proc. Natl Acad. Sci. USA. 55:1966;712-716.
8. Bach R.D., Canepa C., Glukhovtsev M.N. Influence of electrostatic effects on activation barriers in enzymatic reactions: pyridoxal 5′-phosphate-dependent decarboxylation of α-amino acids. J. Am. Chem. Soc. 121:1999;6542-6555.
9. Dunathan H.C., Voet J.G. Stereochemical evidence for the evolution of pyridoxal-phosphate enzymes of various function from a common ancestor. Proc. Natl Acad. Sci. USA. 71:1974;3888-3891.
10. Alexander F.W., Sandmeier E., Metha P.K., Christen P. Evolutionary relationships among pyridoxal-5′-phosphate-dependent enzymes. Eur. J. Biochem. 219:1994;953-960.
11. Grishin N.V., Phillips M.A., Goldsmith E.J. Modelling of the spatial structure of eukaryotic ornithine decarboxylase. Protein Sci. 4:1995;1291-1304.
12. Käck H., Sandmark J., Gibson K., Schneider G., Lindqvist Y. Crystal structure of diamino pelargonic acid synthase; evolutionary relationships between pyridoxal-5′-phosphate dependent enzymes. J. Mol. Biol. 291:1999;857-876.
13. Metha P.K., Hale T.I., Christen P. Aminotransferases: demonstration of homology and division into evolutionary subgroups. Eur. J. Biochem. 214:1993;549-561.
14. 2 multienzyme complex from Salmonella typhimurium. J. Biol. Chem. 263:1988;17857-17871.
15. Gallagher D.T., Eisenstein E.et al. Structure and control of pyridoxal phosphate dependent allosteric threonine deaminase. Structure. 6:1998;465-475.
16. Burkhard P., Rao G.S.J., Hohenester E., Schnackerz K.D., Cook P.F., Jansonius J.N. Three-dimensional structure of O-acetylserine sulfhydrylase from Salmonella typhimurium. J. Mol. Biol. 283:1998;121-133.
17. Shaw J.P., Petsko G.A., Ringe D. Determination of the structure of alanine racemase from Bacillus stearothermophilus at 1.9 Å resolution. Biochemistry. 36:1997;1329-1342.
18. Kern A.D., Oliveira M.A., Coffino P., Hackert M.L. Structure of mammalian decarboxylase at 1.6 Å resolution: stereochemical implications of PLP-dependent amino acid decarboxylases. Structure. 7:1999;567-581.
19. Eswaramoorthy, S., Kycia, H., Gerchman, S., Graziano, V., Studier, W. & Swaminathan, S. (1999). Crystal structure of a yeast hypothetical protein, in press.
20. Sugio S., Petsko G.A., Manning J.M., Soda K., Ringe D. Crystal structure of a D-amino acid aminotransferase: how the protein controls stereoselectivity. Biochemistry. 34:1995;9661-9669.
21. Okada K., Hirotsu K., Sato M., Hayashi H., Kagamiyama H. Three-dimensional structure of Escherichia coli branched-chain amino acid aminotransferase at 2.5 Å resolution. J. Biochem. 122:1997;637-641.
22. Weber I.T., Johnsson L.N., Wilson K.S., Yeates D.G., Wild D.L., Jenkins J.A. Crystallographic studies on the activity of glycogen phosphorylase b. Nature. 274:1978;433-437.
23. Sprang S., Fletterick R.J. The structure of glycogen phosphorylase α at 2.5 Å resolution. J. Mol. Biol. 131:1979;523-551.
24. Rhee S., Parris K.D., Hyde C.C., Ahmed S.A., Wilson Miles E., Davies D.R. Crystal structures of a mutant (βK87T) tryptophan synthase α2β2 complex with ligands bound to the active sites of the α- and β-subunits reveal ligand-induced conformational changes. Biochemistry. 36:1997;7664-7680.
25. Schneider T.R., Gerhard E., Lee M., Liang P.-H., Anderson K.S., Schlichting I. Loop closure and intersubunit communication in tryptophan synthase. Biochemistry. 37:1998;5394-5406.
26. Ford G.C., Eichele G., Jansonius J.N. Three-dimensional structure of a pyridoxal-phosphate-dependent enzyme, mitochondrial aspartate aminotransferase. Proc. Natl Acad. Sci. USA. 77:1980;2559-2563.
27. Malashkevich V.N., Strokopytov B.V., Borisov V.V., Dauter Z., Wilson K.S. Crystal structure of the closed form of chicken cytosolic aspartate aminotransferase at 1.9 Å resolution. J. Mol. Biol. 247:1995;111-124.
28. Arnone A., Rodgers P.H., Hyde C.C., Briley P.D., Metzler C.M., Metzler D.E. Pig cytosolic aspartate aminotransferase: the structure of the internal aldimine, external aldimine and ketimine and of the β subform. Christen P., Metzler D.E. Transaminases. 1985;138-155 John Wiley & Sons, New York.
29. Jäger J., Moser M., Sauder U., Jansonius J.N. Crystal structures of Escherichia coli aspartate aminotransferase in two conformations: comparison of an unliganded open and two liganded closed forms. J. Mol. Biol. 239:1994;285-305.
30. Okamoto A., Higuchi T., Hirotsu K., Kuramitsu S., Kagamiyama H. X-ray crystallographic study of pyridoxal 5′-phosphate-type aspartate aminotransferase from Escherichia coli in open and closed form. J. Biochem. 116:1994;95-107.
31. Jeffery C.J., Barry T., Doonan S., Petsko G.A., Ringe D. Crystal structure of Saccharomyces cerevisiae cytosolic aspartate aminotransferase. Protein Sci. 7:1998;1380-1387.
32. Nakai T., Hirotsu K.et al. Structure of Thermus thermophilus HB8 aspartate aminotransferase and its complex with maleate. Biochemistry. 38:1999;2413-2424.
33. Okamoto A., Nakai Y., Hayashi H., Hirotsu K., Kagamiyama H. Crystal structure of Paracoccus denitrificans aromatic amino acid aminotransferase: a substrate recognition site constructed by rearrangement of hydrogen bond network. J. Mol. Biol. 280:1998;443-461.
34. Blankenfeld W., Nowicki C., Montemartini-Kalisz M., Kalisz H.M., Hecht H.J. Crystal structure of Trypanosoma cruzi tyrosine aminotransferase: substrate specificity is influenced by cofactor binding mode. Protein Sci. 8:1999;2406-2417.
35. Toney M.D., Hohenester E., Cowan S.W., Jansonius J.N. Dialkylglycine decarboxylase structure: bifunctional active site and alkali metal sites. Science. 261:1993;756-759.
36. 6-dependent enzyme with asymmetry in structure and active site reactivity. Proc. Natl Acad. Sci. USA. 94:1997;4866-4871.
37. Shen B.W., Hennig M., Hohenester E., Jansonius J.N., Schirmer T. Crystal structure of human recombinant ornithine aminotransferase. J. Mol. Biol. 277:1998;81-102.
38. Shah S.A., Shen B.W., Brünger A.T. Human ornithine aminotransferase complexed with L-canaline and gubaculine: structural basis for substrate recognition. Structure. 5:1997;1067-1075.
39. Watanabe N., Fukutani H.et al. Crystal structure analysis of ω-amino acid:pyruvate aminotransferase with a newly developed Weissenberg camera and an imaging plate using synchrotron radiation. J. Biochem. 105:1989;1-3.
40. Alexeev D., Alexeeva M., Baxter R., Campopiano D.J., Webster S.P., Sawyer L. The crystal structure of 8-amino-7-oxononanoate synthase: a bacterial PLP-dependent, acyl-CoA-condensing enzyme. J. Mol. Biol. 284:1998;401-419.
41. Storici P., Schirmer T.et al. Crystal structure of GABA-aminotransferase, a target for antiepileptic drug therapy. Biochemistry. 38:1999;8628-8634.
42. Hester G., Stark W., Moser M., Kallen J., Markovic-Housley Z., Jansonius J. Crystal structure of phosphoserine aminotransferase from Escherichia coli at 2.3 Å resolution: comparison of the unligated enzyme and a complex with α-methyl-1-glutamate. J. Mol. Biol. 286:1999;829-850.
43. Antson A.A., Wilson K.S.et al. Three-dimensional structure of tyrosine phenol-lyase. Biochemistry. 32:1993;4195-4206.
44. Pletnev S.V., Arutyunyan E.G.et al. Crystallographic study of tyrosine phenole-lyase from Erwinia herbicola. Crystallography reports. 42:1997;809-819.
45. Isupov M.N., Harutyunyan E.H.et al. Crystal structure of tryptophanase. J. Mol. Biol. 276:1998;603-623.
46. Clausen T., Huber R., Laber B., Pohlenz H.D., Messerschmidt A. Crystal structure of the pyridoxal-5′-phosphate dependent cystathionine β-lyase from Escherichia coli at 1.83 Å J. Mol. Biol. 262:1996;202-224.
47. Clausen T., Huber R., Prade L., Wahl M.C., Messerschmidt A. Crystal structure of Escherichia coli cystathionine γ-synthase at 1.5 Å resolution. EMBO J. 17:1998;6827-6838.
48. Momany C., Ernst S., Ghosh R., Chang N.L., Hackert M.L. Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 Å resolution. J. Mol. Biol. 252:1995;643-655.
49. Renwick S.B., Snell K., Baumann U. The crystal structure of human cytosolic serine hydroxymethyltransferase: a target for cancer chemotherapy. Structure. 6:1998;1105-1116.
50. Scarsdale J.N., Kazanina G., Radeev S., Schirch V., Wright H.T. Crystal structure of rabbit cytosolic serine hydroxymethyltransferase at 2.8 Å resolution: mechanistic implications. Biochemistry. 38:1999;8347-8358.
51. Eads J.C., Beeby M., Scapin G., Yu T.-W., Floss H.G. Crystal structure of 3-amino-5-hydroxybenzoic acid synthase. Biochemistry. 38:1999;9840-9849.
52. O'Reilly M., Watson K.A., Schinzel R., Palm D., Johnson L.N. Oligosaccharide substrate binding in Escherichia coli maltodextrin phosphorylase. Nat. Struct. Biol. 4:1997;405-412.