Molecular cloning of the aspartate 4-decarboxylase gene from Pseudomonas sp. ATCC 19121 and characterization of the bifunctional recombinant enzyme

Applied Microbiology and Biotechnology

Volumn 73, Issue 2, 2006, Pages 339-348

  Wang, Nai Chen ^a   Lee, Chia Yin ^a  

^a NATIONAL TAIWAN UNIVERSITY   (Taiwan)

Author keywords

[No Author keywords available]

Indexed keywords

BIFUNCTIONAL RECOMBINANT ENZYME; GRAM-POSITIVE MICROBES; MOLECULAR CLONING; PSEUDOMONAS STRAIN;

CLONING; ENZYMES; ESCHERICHIA COLI; GENES; KINETIC PARAMETERS; MOLECULAR MASS; PH EFFECTS;

MICROBIOLOGY;

AMINO ACID DERIVATIVE; AMINOTRANSFERASE; ASPARTATE BETA DECARBOXYLASE; BACTERIAL ENZYME; DIVALENT CATION; RECOMBINANT ENZYME; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG; ASPARTATE 4-DECARBOXYLASE; CARBOXYLYASE;

AMINO ACID; BACTERIUM; CLONE; ENZYME ACTIVITY; INDUSTRIAL PRODUCTION; MOLECULAR ANALYSIS; PH; PROTEIN; RECOMBINATION;

ARTICLE; BACTERIAL STRAIN; BACTERIUM CULTURE; CARBOXY TERMINAL SEQUENCE; DECARBOXYLATION; ENZYME ACTIVITY; ESCHERICHIA COLI; GEL FILTRATION; KINETICS; MOLECULAR CLONING; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PROTEIN EXPRESSION; PSEUDOMONAS; AMINO ACID SEQUENCE; BIOSYNTHESIS; CHEMISTRY; ENZYME SPECIFICITY; GEL CHROMATOGRAPHY; GENETICS; METABOLISM; MOLECULAR GENETICS; PHYLOGENY; PLASMID; SEQUENCE HOMOLOGY; TEMPERATURE; TIME;

ESCHERICHIA COLI; POSIBACTERIA; PSEUDOMONAS; PSEUDOMONAS SP. ATCC 19121;

AMINO ACID SEQUENCE; CARBOXY-LYASES; CHROMATOGRAPHY, GEL; CLONING, MOLECULAR; ESCHERICHIA COLI; HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR SEQUENCE DATA; PHYLOGENY; PLASMIDS; PSEUDOMONAS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY; TEMPERATURE; TIME FACTORS; TRANSAMINASES;

EID: 33947389556     PISSN: 01757598     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00253-006-0475-6     Document Type: Article

References (22)

1. Abe K, Ohnishi F, Yagi K, Nakajima T, Higuchi T, Sano M, Machida M, Sarker RI, Maloney PC (2002) Plasmid-encoded asp operon confers a proton motive metabolic cycle catalyzed by an aspartate-alanine exchange reaction. J Bacteriol 184:2906-2913
2. Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ (1997) Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 25:3389-3402
3. Bowers WF, Czubaroff VB, Haschemeyer RH (1970) Subunit structure of L-aspartate β-decarboxylase from Alcaligenes faecalis. Biochemistry 9:2620-2625
4. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
5. Chen CC, Chou TL, Lee CY (2000) Cloning, expression and characterization of L-aspartate β-decarboxylase gene from Alcaligenes faecalis CCRC 11585. J Ind Microbiol 25:132-140
6. Chibata I, Kakimoto T, Kato J (1965) Enzymatic production of L-alanine by Pseudomonas dacunhae. Appl Microbiol 13:638-645
7. Crawford LV (1958) Studies on the aspartic decarboxylase of Nocardia globerula. Biochem J 68:221-225
8. Dimroth P, Schink B (1998) Energy conservation in the decarboxylation of dicarboxylic acids by fermenting bacteria. Arch Microbiol 170:69-77
9. Dogan B, Boor KJ (2003) Genetic diversity and spoilage potentials among Pseudomonas spp. isolated from fluid milk products and dairy processing plants. Appl Environ Microbiol 69:130-138
10. Dunathan HC (1966) Conformation and reaction specificity in pyridoxal phosphate enzymes. Proc Natl Acad Sci USA 55:712-716
11. El-Rahmany TA (1994) Comparison of L-aspartate 4-carboxy-lyases of Cunninghamella elegans and Penicillium citrinum. Microbiol Res 149:253-257
12. Graber R, Kasper P, Malashkevich VN, Strop P, Gehring H, Jansonius JN, Christen P (1999) Conversion of aspartate aminotransferase into an L-aspartate β-decarboxylase by a triple active-site mutation. J Biol Chem 274:31203-31208
13. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
14. Nishimura JS, Manning JM, Meister A (1962) Studies on the mechanism of activation of aspartic acid β-decarboxylase by α-keto acids and pyridoxal 5′-phosphate. Biochemistry 1:442-447
15. Novogrodsky A, Nishimura JS, Meister A (1963) Transamination and β-decarboxylation of aspartate catalyzed by the same pyridoxal phosphate-enzyme. J Biol Chem 238:PC1903-PC1905
16. Rathod PK, Fellman JH (1985) Identification of mammalian aspartate-4-decarboxylase. Arch Biochem Biophys 238:435-446
17. Rozzell JD (1991) Method and compositions for the production of L-alanine and derivatives. US Patent No. 5,019,509
18. Saitou N, Nei M (1987) The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol 4:406-425
19. Sambrook J, Fritsch EF, Manniatis T (1989) Molecular cloning: a laboratory manual. Cold Spring Harbor Laboratory Press, New York
20. Tate ST, Meister A (1970) Regulation and subunit structure of aspartate β-decarboxylase. Studies on the enzymes from Alcaligenes faecalis and Pseudomonas dacunhae. Biochemistry 9:2626-2632
21. Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG (1997) The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 25:4876-4882
22. Wilson EM, Kornberg HL (1963) Properties of crystalline L-aspartate 4-carboxy-lyase from Achromobacter sp. Biochem J 88:578-587