Cloning and characterization of GL-7-ACA acylase gene from Pseudomonas sp. GK16

Youngsik Lee, Han Chul Yang, Sung Soo Park

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The gene coding for glutaryl-7-aminocephalosporanic acid (GL-7-ACA) acylase was cloned from Pseudomonas sp. GK16 and some of its characteristics were analyzed. The complete nucleotide sequence revealed that the putative open reading frame is 2160 bases long and encodes 720 amino acids. By SDS-PAGE three proteins, approximately corresponding to 70, 54 and 16 kDa of molecular weight, were detected in E. coli cells carrying pGAP18. The largest protein should be a precursor which is not processed yet, while the other two proteins must be derived from the precursor by the proteolytic processing.

Original languageEnglish
Pages (from-to)375-380
Number of pages6
JournalJournal of Microbiology and Biotechnology
Volume6
Issue number6
Publication statusPublished - 1996 Dec 1

Fingerprint

amidase
Cloning
Pseudomonas
Organism Cloning
Genes
Proteins
Acids
Nucleotides
Escherichia coli
Open Reading Frames
Amino acids
Polyacrylamide Gel Electrophoresis
Molecular Weight
Molecular weight
Amino Acids
Processing
glutaryl-7-aminocephalosporanic acid

Keywords

  • Cloning
  • Expression
  • GL-7-ACA acylase
  • Nucleotide sequence
  • Processing
  • Pseudomonas sp. GK16

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology
  • Microbiology

Cite this

Cloning and characterization of GL-7-ACA acylase gene from Pseudomonas sp. GK16. / Lee, Youngsik; Yang, Han Chul; Park, Sung Soo.

In: Journal of Microbiology and Biotechnology, Vol. 6, No. 6, 01.12.1996, p. 375-380.

Research output: Contribution to journalArticle

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