Characterization of two bacterial hydroxynitrile lyases with high similarity to cupin superfamily proteins

Applied and Environmental Microbiology

Volumn 78, Issue 6, 2012, Pages 2053-2055

  Hussain, Zahid ^a,d   Wiedner, Romana ^a,b   Steiner, Kerstin ^b   Hajek, Tanja ^a,b   Avi, Manuela ^a,e   Hecher, Bianca ^b,f   Sessitsch, Angela ^c   Schwab, Helmut ^a,b  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^b AUSTRIAN CENTRE OF INDUSTRIAL BIOTECHNOLOGY   (Austria)

^c AIT AUSTRIAN INSTITUTE OF TECHNOLOGY   (Austria)

^d GC UNIVERSITY   (Pakistan)

^e NOVARTIS PHARMA AG   (Switzerland)

^f ProtAffin Biotechnologie AG   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

CARBON-CARBON BOND; ENANTIOSELECTIVE; ENDOPHYTIC BACTERIA; HYDROCYANIC ACID; HYDROXYNITRILE LYASES; REVERSE REACTIONS; SYNTHESIS REACTION;

ALDEHYDES; ENANTIOSELECTIVITY; ENZYMES; PROTEINS;

BIOSYNTHESIS;

ACETONITRILE DERIVATIVE; BACTERIAL DNA; BENZALDEHYDE; BENZALDEHYDE DERIVATIVE; LYASE; MANDELONITRILE;

BACTERIUM; CATALYSIS; ENDOPHYTE; FUNCTIONAL GROUP; PROTEIN;

ARTICLE; BACTERIUM; CHEMISTRY; DNA SEQUENCE; ENDOPHYTE; ENZYMOLOGY; GENETICS; METABOLISM; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; SEQUENCE HOMOLOGY;

ACETONITRILES; BACTERIA; BENZALDEHYDES; DNA, BACTERIAL; ENDOPHYTES; LYASES; MOLECULAR SEQUENCE DATA; SEQUENCE ANALYSIS, DNA; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS);

EID: 84857820887     PISSN: 00992240     EISSN: 10985336     Source Type: Journal    
DOI: 10.1128/AEM.06899-11     Document Type: Article

References (21)

1. Agarwal G, Rajavel M, Gopal B, Srinivasan N. 2009. Structure-based phylogeny as a diagnostic for functional characterization of proteins with a cupin fold. PLoS One 4:e5736.
2. Blumer C, Haas D. 2000. Mechanism, regulation, and ecological role of bacterial cyanide biosynthesis. Arch. Microbiol. 173:170-177.
3. Dadashipour M, Asano Y. 2011. Hydroxynitrile lyases: insights into biochemistry, discovery and engineering. ACS Catal. 1:1121-1149.
4. Dreveny I, Andryushkova AS, Glieder A, Gruber K, Kratky C. 2009. Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity. Biochemistry 48:3370-3377.
5. Duffy B, Keel C, Defago G. 2004. Potential role of pathogen signaling in multitrophic plant-microbe interactions involved in disease protection. Appl. Environ. Microbiol. 70:1836-1842.
6. Dunwell JM, Purvis A, Khuri S. 2004. Cupins: the most functionally diverse protein superfamily? Phytochemistry 65:7-17.
7. Gane PJ, Dunwell JM, Warwicker J. 1998. Modeling based on the structure of vicilins predicts a histidine cluster in the active site of oxalate oxidase. J. Mol. Evol. 46:488-493.
8. Hasslacher M, Kratky C, Griengl H, Schwab H, Kohlwein S. 1997. Hydroxynitrile lyase from Hevea brasiliensis: molecular characterization and mechanism of enzyme catalysis. Proteins 27:438-449.
9. Holt J, Hanefeld U. 2010. Enantioselective enzyme-catalysed synthesis of cyanohydrins. Curr. Org. Synth. 6:15-37.
10. Krammer B, Rumbold K, Tschemmernegg M, Pöchlauer P, Schwab H. 2007. A novel screening assay for hydroxynitrile lyases suitable for highthroughput screening. J. Biotechnol. 129:151-161.
11. Purkarthofer T, Skranc W, Schuster C, Griengl H. 2007. Potential and capabilities of hydroxynitrile lyases as biocatalysts in the chemical industry. Appl. Microbiol. Biotechnol. 76:309-320.
12. Reisinger C, Kern A, Fesko K, Schwab H. 2007. An efficient plasmid vector for expression cloning of large numbers of PCR fragments in Escherichia coli. Appl. Microbiol. Biotechnol. 77:241-244.
13. Reiter B, Pfeifer U, Schwab H, Sessitsch A. 2002. Response of endophytic bacterial communities in potato plants to infection with Erwinia carotovora subsp. atroseptica. Appl. Environ. Microbiol. 68:2261-2268.
14. Ryan RP, Germaine K, Franks A, Ryan DJ, Dowling DN. 2008. Bacterial endophytes: recent developments and applications. FEMS Microbiol. Lett. 278: 1-9.
15. Sessitsch A, Reiter B, Berg G. 2004. Endophytic bacterial communities of field-grown potato plants and their plant-growth-promoting and antagonistic abilities. Can. J. Microbiol. 50:239-249.
16. Sulzbacher Caruso C, et al. 2009. α-Hydroxynitrile lyase protein from Xylella fastidiosa: cloning, expression, and characterization. Microb. Pathog. 47:118-127.
17. 2+-containing hydroxynitrile lyase from flax (Linum usitatissimum) in Pichia pastoris-utilization of the recombinant enzyme for enzymatic analysis and site-directed mutagenesis. Plant Sci. 139:19-27.
18. Wajant H, Mundry KW, Pfizenmaier K. 1994. Molecular cloning of hydroxynitrile lyase from Sorghum bicolor (L.): homologies to serine carboxypeptidases. Plant Mol. Biol. 26:735-746.
19. Winkler M, Glieder A, Steiner K. Hydroxynitrile lyases: from nature to application. In Carriera E, Yamamoto H (ed), Comprehensive chirality, vol 7: Synthetic methods VI-enzymatic and semi-enzymatic. Elsevier, in press.
20. Zagrobelny M, Bak S, Moeller B. 2008. Cyanogenesis in plants and arthropods. Phytochemistry 69:1457-1468.
21. Zinniel DK, et al. 2002. Isolation and characterization of endophytic colonizing bacteria from agronomic crops and prairie plants. Appl. Environ. Microbiol. 68:2198-2208.