α-amino-β-carboxymuconic-ε-semialdehyde decarboxylase (ACMSD) is a new member of the amidohydrolase superfamily

Biochemistry

Volumn 45, Issue 21, 2006, Pages 6628-6634

  Li, Tingfeng ^a   Iwaki, Hiroaki ^b   Fu, Rong ^a   Hasegawa, Yoshie ^b   Zhang, Hong ^c   Liu, Aimin ^a  

^a UNIVERSITY OF MISSISSIPPI MEDICAL CENTER   (United States)

^b KANSAI UNIVERSITY   (Japan)

^c UNIVERSITY OF TEXAS SOUTHWESTERN MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ELECTRONIC STRUCTURE; FLUORESCENCE; KINETIC ENERGY; PROTEINS; REDUCTION;

AMIDOHYDROLASE; CATALYTIC MECHANISMS; COFACTORS; SEMIALDEHYDE DECARBOXYLASE (ACMSD);

ENZYMES;

ALPHA AMINO BETA CARBOXYMUCONIC EPSILON SEMIALDEHYDE DECARBOXYLASE; BACTERIAL ENZYME; CARBOXYLYASE; COBALT CHLORIDE; DNA; HYDROLASE; LIGAND; METAL ION; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; KINETICS; MUTAGENESIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PLASMID; POLYMERASE CHAIN REACTION; PRIORITY JOURNAL; PSEUDOMONAS FLUORESCENS; STEADY STATE; ULTRAVIOLET SPECTROSCOPY;

AMIDOHYDROLASES; AMINO ACID SEQUENCE; BASE SEQUENCE; CARBOXY-LYASES; DNA PRIMERS; ESCHERICHIA COLI; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; PLASMIDS; SEQUENCE HOMOLOGY, AMINO ACID;

PSEUDOMONAS FLUORESCENS;

EID: 33744728709     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060108c     Document Type: Article

References (37)

1. Mehler, A. H. (1956) Formation of picolinic and quinolinic acids following enzymatic oxidation of 3-hydroxyanthranilic acid, J. Biol. Chem. 218, 241-254.
2. Nishizuka, Y., Ichiyama, A., and Hayaishi, O. (1970) Metabolism of the benzene ring of tryptophan (mammals), Methods Enzymol. 17, 463-466.
3. Fukuoka, S., Ishiguro, K., Yanagihara, K., Tanabe, A., Egashira, Y., Sanada, H., and Shibata, K. (2002) Identification and expression of a cDNA encoding human α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD). A key enzyme for the tryptophan-niacine pathway and "quinolinate hypothesis", J. Biol. Chem. 277, 35162-35167.
4. Tanabe, A., Egashira, Y., Fukuoka, S., Shibata, K., and Sanada, H. (2002) Purification and molecular cloning of rat 2-amino-3-carboxymuconate-6- semialdehyde decarboxylase, Biochem. J. 361, 567-575.
5. Muraki, T., Taki, M., Hasegawa, Y., Iwaki, H., and Lau, P. C. (2003) Prokaryotic homologs of the eukaryotic 3-hydroxyanthranilate 3,4-dioxygenase and 2-amino-3-carboxymuconate-6-semialdehyde decarboxylase in the 2-nitrobenzoate degradation pathway of Pseudomonas fluorescens strain KU-7, Appl. Environ. Microbiol. 69, 1564-1572.
6. Horton, R. M. (1995) PCR-mediated recombination and mutagenesis. SOEing together tailor-made genes, Mol. Biotechnol. 3, 93-99.
7. Koontz, W. A., and Shiman, R. (1976) Beef kidney 3-hydroxyanthranilic acid oxygenase. Purification, characterization, and analysis of the assay, J. Biol. Chem. 251, 368-377.
8. Marchler-Bauer, A., Anderson, J. B., DeWeese-Scott, C., Fedorova, N. D., Geer, L. Y., He, S., Hurwitz, D. I., Jackson, J. D., Jacobs, A. R., Lanczycki, C. J., Liebert, C. A., Liu, C., Madej, T., Marchler, G. H., Mazumder, R., Nikolskaya, A. N., Panchenko, A. R., Rao, B. S., Shoemaker, B. A., Simonyan, V., Song, J. S., Thiessen, P. A., Vasudevan, S., Wang, Y., Yamashita, R. A., Yin, J. J., and Bryant, S. H. (2003) CDD: a curated Entrez database of conserved domain alignments, Nucleic Acids Res. 31, 383-387.
9. Bateman, A., Coin, L., Durbin, R., Finn, R. D., Hollich, V., Griffiths-Jones, S., Khanna, A., Marshall, M., Moxon, S., Sonnhammer, E. L., Studholme, D. J., Yeats, C., and Eddy, S. R. (2004) The Pfam protein families database, Nucleic Acids Res. 32, D138-D141.
10. Altschul, S. F., Madden, T. L., Schaffer, A. A., Zhang, J., Zhang, Z., Miller, W., and Lipman, D. J. (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs, Nucleic Acids Res. 25, 3389-3402.
11. Pei, J., Sadreyev, R., and Grishin, N. V. (2003) PCMA: fast and accurate multiple sequence alignment based on profile consistency, Bioinformatics 19, 427-428.
12. McGuffin, L. J., Bryson, K., and Jones, D. T. (2000) The PSIPRED protein structure prediction server, Bioinformatics 16, 404-405.
13. Fukuwatari, T., Ohsaki, S., Fukuoka, S.-i., Sasaki, R., and Shibata, K. (2004) Phthalate esters enhance quinolinate production by inhibiting α-amino-β-carboxymuconate-ε-semialdehyde decarboxylase (ACMSD), a key enzyme of the tryptophan pathway, Toxicol. Sci. 81, 302-308.
14. Mehler, A. H., Mc, D. E., and Hundley, J. M. (1958) Changes in the enzymatic composition of liver. I. Increase of picolinic carboxylase in diabetes, J. Biol. Chem. 232, 323-330.
15. Tatusov, R. L., Fedorova, N. D., Jackson, J. D., Jacobs, A. R., Kiryutin, B., Koonin, E. V., Krylov, D. M., Mazumder, R., Mekhedov, S. L., Nikolskaya, A. N., Rao, B. S., Smirnov, S., Sverdlov, A. V., Vasudevan, S., Wolf, Y. I., Yin, J. J., and Natale, D. A. (2003) The COG database: an updated version includes eukaryotes, BMC Bioinformatics 4, 41.
16. Holm, L., and Sander, C. (1997) An evolutionary treasure: unification of a broad set of amidohydrolases related to urease, Proteins 28, 72-82.
17. Seibert, C. M., and Raushel, F. M. (2005) Structural and catalytic diversity within the amidohydrolase superfamily, Biochemistry 44, 6383-6391.
18. Gerlt, J. A., and Babbitt, P. C. (2001) Divergent evolution of enzymatic function: mechanistically diverse superfamilies and functionally distinct suprafamilies, Annu. Rev. Biochem. 70, 209-246.
19. Wackett, L. P. (2004) Evolution of enzymes for the metabolism of new chemical inputs into the environment, J. Biol. Chem. 279, 41259-41262.
20. Gerlt, J. A., and Raushel, F. M. (2003) Evolution of function in (beta/alpha)8-barrel enzymes, Curr. Opin. Chem. Biol. 7, 252-264.
21. Sterner, R., and Hocker, B. (2005) Catalytic versatility, stability, and evolution of the (beta/alpha)8-barrel enzyme fold, Chem. Rev. 105, 4038-4055.
22. Porter, T. N., Li, Y., and Raushel, F. M. (2004) Mechanism of the dihydroorotase reaction, Biochemistry 43, 16285-16292.
23. Hausinger, R. P. (2000) Kinetic and structural characterization of urease active site variants, Biochemistry 39, 8575-8584.
24. Thoden, J. B., Phillips, G. N., Jr., Neal, T. M., Raushel, F. M., and Holden, H. M. (2001) Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center, Biochemistry 40, 6989-6997.
25. Wang, Z., and Quiocho, F. A. (1998) Complexes of adenosine deaminase with two potent inhibitors: X-ray structures in four independent molecules at pH of maximum activity, Biochemistry 37, 8314-8324.
26. Wilson, D. K., Rudolph, F. B., and Quiocho, F. A. (1991) Atomic structure of adenosine deaminase complexed with a transition-state analog: understanding catalysis and immunodeficiency mutations, Science 252, 1278-1284.
27. Wilson, D. K., and Quiocho, F. A. (1994) Crystallographic observation of a trapped tetrahedral intermediate in a metalloenzyme, Nat. Struct. Biol. 1, 691-694.
28. Jabri, E., Carr, M. B., Hausinger, R. P., and Karplus, P. A. (1995) The crystal structure of urease from Klebsiella aerogenes, Science 268, 998-1004.
29. Palmatier, R. D., McCroskey, R. P., and Abbott, M. T. (1970) The enzymatic conversion of uracil 5-carboxylic acid to uracil and carbon dioxide, J. Biol. Chem. 245, 6706-6710.
30. Smiley, J. A., Kundracik, M., Landfried, D. A., Barnes, V. R., Sr., and Axhemi, A. A. (2005) Genes of the thymidine salvage pathway: Thymine-7-hydroxylase from a Rhodotorula glutinis cDNA library and iso-orotate decarboxylase from Neurospora crassa, Biochim. Biophys. Acta 1723, 256-264.
31. Feng, D.-F., Cho, G., and Doolittle, R. F. (1997) Determining divergence times with a protein clock: Update and reevaluation, Proc. Natl. Acad. Sci. U.S.A. 94, 13028-13033.
32. Ireton, G. C., McDermott, G., Black, M. E., and Stoddard, B. L. (2002) The structure of Escherichia coli cytosine deaminase, J. Mol. Biol. 315, 687-697.
33. Liaw, S. H., Chen, S. J., Ko, T. P., Hsu, C. S., Chen, C. J., Wang, A. H., and Tsai, Y. C. (2003) Crystal structure of D-aminoacylase from Alcaligenes faecalis DA1. A novel subset of amidohydrolases and insights into the enzyme mechanism, J. Biol. Chem. 278, 4957-4962.
34. Nitanai, Y., Satow, Y., Adachi, H., and Tsujimoto, M. (2002) Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis, J. Mol. Biol. 321, 177-184.
35. Pearson, M. A., Michel, L. O., Hausinger, R. P., and Karplus, P. A. (1997) Structures of Cys319 variants and acetohydroxamate-inhibited Klebsiella aerogenes urease, Biochemistry 36, 8164-8172.
36. Thoden, J. B., Marti-Arbona, R., Raushel, F. M., and Holden, H. M. (2003) High-resolution X-ray structure of isoaspartyl dipeptidase from Escherichia coli, Biochemistry 42, 4874-4882.
37. Benning, M. M., Kuo, J. M., Raushel, F. M., and Holden, H. M. (1995) Three-dimensional structure of the binuclear metal center of phosphotriesterase, Biochemistry 34, 7973-7978.