Novel metal-binding site of Pseudomonas reinekei MT1 trans-dienelactone hydrolase

Biochemical and Biophysical Research Communications

Volumn 390, Issue 4, 2009, Pages 1345-1348

  Marín, Macarena ^a   Pieper, Dietmar H ^a  

^a HELMHOLTZ CENTRE FOR INFECTION RESEARCH   (Germany)

Author keywords

Biodegradation; Dienelactone hydrolase; PF04199; Pseudomonas reinekei; Trinulear metal binding motif; Zinc dependent hydrolase

Indexed keywords

AMINO ACID; HYDROLASE; MALEYLACETATE REDUCTASE; MANGANESE; PROTOANEMONIN; TRANS DIENELACTONE HYDROLASE; UNCLASSIFIED DRUG; ZINC ION;

ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CONTROLLED STUDY; ENZYME ACTIVITY; METAL BINDING; NONHUMAN; PRIORITY JOURNAL; PSEUDOMONAS; PSEUDOMONAS REINEKEI;

BINDING SITES; CARBOXYLIC ESTER HYDROLASES; CATECHOLS; CATIONS, DIVALENT; MANGANESE; PROTEIN STRUCTURE, SECONDARY; PSEUDOMONAS; ZINC;

PSEUDOMONAS;

EID: 70450239586     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.10.151     Document Type: Article

References (18)

1. Pieper D., and Reineke W. In: Ramos J.L. (Ed). Degradation of Chloroaromatics by Pseudomona(d)s in Pseudomonas (2004), Kluwer Academic/Plenum Publishers, New York 509-574
2. Dorn E., and Knackmuss H.-J. Chemical structure and biodegradability of halogenated aromatic compounds: two catechol 1,2-dioxygenases from a 3-chlorobenzoate-grown pseudomonad. Biochem. J. 174 (1978) 73-84
3. Schmidt E., and Knackmuss H.-J. Chemical structure and biodegradability of halogenated aromatic compounds: conversion of chlorinated muconic acids into maleoylacetic acid. Biochem. J. 192 (1980) 339-347
4. Kaschabek S.R., and Reineke W. Maleylacetate reductase of Pseudomonas sp. strain B13: dechlorination of chloromaleylacetates, metabolites in the degradation of chloroaromatic compounds. Arch Microbiol. 158 (1992) 412-417
5. Camara B., Nikodem P., Bielecki P., Bobadilla R., Junca H., and Pieper D.H. Characterization of a gene cluster involved in 4-chlorocatechol degradation by Pseudomonas reinekei MT1. J. Bacteriol. 189 (2009) 1664-1674
6. Camara B., Marin M., Schlomann M., Hecht H.J., Junca H., and Pieper D.H. trans-Dienelactone hydrolase from Pseudomonas reinekei MT1, a novel zinc-dependent hydrolase. Biochem. Biophys. Res. Commun. 376 (2008) 423-428
7. Schlömann M., Schmidt E., and Knackmuss H.-J. Different types of dienelactone hydrolase in 4-fluorobenzoate-utilizing bacteria. J. Bacteriol. 172 (1990) 5112-5118
8. 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. The Pfam protein families database. Nucleic Acids Res. 32 (2004) D138-D141
9. Nikodem P., Hecht V., Schlömann M., and Pieper D.H. New bacterial pathway for 4- and 5-chlorosalicylate degradation via 4-chlorocatechol and maleylacetate in Pseudomonas sp. strain MT1. J. Bacteriol. 185 (2003) 6790-6800
10. Reineke W., and Knackmuss H.-J. Microbial metabolism of haloaromatics: isolation and properties of a chlorobenzene-degrading bacterium. Appl. Environ. Microbiol. 47 (1984) 395-402
11. Bradford M.M. A rapid and sensitive method for the quantitation of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
12. Larsen K.S., and Auld D.S. Carboxypeptidase A: mechanism of zinc inhibition. Biochemistry 28 (1989) 9620-9625
13. Yoshimoto T., Tanaka N., Kanada N., Inoue T., Nakajima Y., Haratake M., Nakamura K.T., Xu Y., and Ito K. Crystal structures of creatininase reveal the substrate binding site and provide an insight into the catalytic mechanism. J. Mol. Biol. 337 (2004) 399-416
14. McCall K.A., Huang C., and Fierke C.A. Function and mechanism of zinc metalloenzymes. J. Nutr. 130 (2000) 1437S-1446S
15. Hough E., Hansen L.K., Birknes B., Jynge K., Hansen S., Hordvik A., Little C., Dodson E., and Derewenda Z. High-resolution (1.5 Å) crystal structure of phospholipase C from Bacillus cereus. Nature 338 (1989) 357-360
16. Volbeda A., Lahm A., Sakiyama F., and Suck D. Crystal structure of Penicillium citrinum P1 nuclease at 2.8 Å resolution. EMBO J. 10 (1991) 1607-1618
17. Kim E.E., and Wyckoff H.W. Reaction mechanism of alkaline phosphatase based on crystal structures. Two-metal ion catalysis. J. Mol. Biol. 218 (1991) 449-464
18. Bone R., Frank L., Springer J.P., and Atack J.R. Structural studies of metal binding by inositol monophosphatase: evidence for two-metal ion catalysis. Biochemistry 33 (1994) 9468-9476