Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 67, 2003 - Issue 1
Journal homepage
296
Views
8
CrossRef citations to date
0
Altmetric
Original Articles

Functions of Malonate Decarboxylase Subunits from Pseudomonas putida

Shigeru CHOHNANDepartment of Bioresource Science, College of Agriculture, Ibaraki University 3-21-1 Chuo, Ami, Ibaraki 300-0393, Japan
,
Kayo AKAGIDepartment of Bioresource Science, College of Agriculture, Ibaraki University 3-21-1 Chuo, Ami, Ibaraki 300-0393, Japan
&
Yoshichika TAKAMURADepartment of Bioresource Science, College of Agriculture, Ibaraki University 3-21-1 Chuo, Ami, Ibaraki 300-0393, Japan
Pages 214-217 | Received 29 Aug 2002, Accepted 02 Oct 2002, Published online: 22 May 2014

  • 1) Takamura, Y., and Kitayama, Y., Purification and some properties of malonate decarboxylase from Pseudomonas ovalis: an oligomeric enzyme with bifunctional properties. Biochem. Int., 3, 483-491 (1981).
  • 2) Chohnan, S., Fujio, T., Takaki, T., Yonekura, M., Nishihara, H., and Takamura, Y., Malonate decarboxylase of Pseudomonas putida is composed of five subunits. FEMS Microbiol. Lett., 169, 37-43 (1998).
  • 3) Chohnan, S., Kurusu, Y., Nishihara, H., and Takamura, Y., Cloning and characterization of mdc genes encoding malonate decarboxylase from Pseudomonas putida. FEMS Microbiol. Lett., 174, 311-319 (1999).
  • 4) Schmid, M., Berg, M., Hilbi, H., and Dimroth, P., Malonate decarboxylase of Klebsiella pneumoniae catalyses the turnover of acetyl and malonyl thioester residues on a coenzyme-A-like prosthetic group. Eur. J. Biochem., 237, 221-228 (1996).
  • 5) Hoenke, S., Schmid, M., and Dimroth, P., Sequence of a gene cluster from Klebsiella pneumoniae encoding malonate decarboxylase and expression of the enzyme in Escherichia coli. Eur. J. Biochem., 246, 530-538 (1997).
  • 6) Hoenke, S., and Dimroth, P., Formation of catalytically active S-acetyl(malonate decarboxylase) requires malonyl-CoA. Eur. J. Biochem., 259, 181-187 (1999).
  • 7) Hilbi, H., Dehning, I., Schink, B., and Dimroth, P., Malonate decarboxylase of Malonomonas rubra, a novel type of biotin-containing acetyl enzyme. Eur. J. Biochem., 207, 117-123 (1992).
  • 8) Hilbi, H., and Dimroth, P., Purification and characterization of a cytoplasmic enzyme component of the Na+-activated malonate decarboxylase system of Malonomonas rubra: acetyl-S-acyl carrier protein:malonate acyl carrier protein-SH transferase. Arch. Microbiol., 164, 48-56 (1994).
  • 9) Berg, M., Hilbi, H., and Dimroth, P., The acyl carrier protein of malonate decarboxylase of Malonomonas rubra contains 2′-(5″-phosphoribosyl)-3′-dephosphocoenzyme A as a prosthetic group. Biochemistry, 35, 4689-4696 (1996).
  • 10) Berg, M., Hilbi, H., and Dimroth, P., Sequence of a gene cluster from Malonomonas rubra encoding components of the malonate decarboxylase Na+ pump and evidence for their function. Eur. J. Biochem., 245, 103-115 (1997).
  • 11) Kim, Y. S., and Byun, H. S., Purification and properties of a novel type of malonate decarboxylase from Acinetobacter calcoaceticus. J. Biol. Chem., 269, 29636-29641 (1994).
  • 12) Koo, J. H., Jung, S. B., Byun, H. S., and Kim, Y. S., Cloning and sequencing of genes encoding malonate decarboxylase in Acinetobacter calcoaceticus. Biochim. Biophys. Acta, 1354, 49-54 (1997).
  • 13) Byun, H. S., and Kim, Y. S., Subunit organization of bacterial malonate decarboxylases: the smallest δ subunit as an acyl-carrier protein. J. Biochem. Mol. Biol., 30, 132-137 (1997).
  • 14) Koo, J. H., and Kim, Y. S., Functional evaluation of the genes involved in malonate decarboxylation by Acinetobacter calcoaceticus. Eur. J. Biochem., 266, 683-690 (1999).
  • 15) Kim, Y. S., and Kim, E. J., A plasmid responsible for malonate assimilation in Pseudomonas fluorescens. Plasmid, 32, 219-221 (1994).
  • 16) Yasukawa, T., Kanei-Ishii, C., Maekawa, T., Fujimoto, J., Yamamoto, T., and Ishii, S., Increase of solubility of foreign proteins in Escherichia coli by coproduction of the bacterial thioredoxin. J. Biol. Chem., 270, 25328-25331 (1995).
  • 17) Machida, S., Yu, Y., Singh, S. P., Kim, J.-D., Hayashi, K., and Kawata, Y., Overproduction of β-glucosidase in active form by an Escherichia coli system coexpressing the chaperonin GroEL/ES. FEMS Microbiol. Lett., 159, 41-46 (1998).
  • 18) Sambrook, J., Fritsch, E. F., and Maniatis, T., Molecular cloning: a laboratory manual, 2nd ed., Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY (1989).
  • 19) Yanisch-Perron, C., Vieira, J., and Messing, J., Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors. Gene, 33, 103-119 (1985).
  • 20) Vieira, J., and Messing, J., Production of single-stranded plasmid DNA. Methods Enzymol., 153, 3-11 (1987).
  • 21) Amann, E., Ochs, B., and Abel, K. J., Tightly regulated tac promoter vectors useful for the expression of unfused and fused proteins in Escherichia coli. Gene, 69, 301-315 (1988).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.