Human aldolase b: Liver-specific properties of the isozyme depend on type b isozyme group-specific sequences

Takahiro Kusakabe, Kiyohisa Motoki, Yasushi Sugimoto, Yozo Takasaki, Katsuji Hori

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

A series of chimeric enzymes between two human aldolases A, B or C were constructed to identify the molecular regions responsible for isozyme-specific functions. Chimeras constructed between aldolases A and B were AB34 (an AB chimera connected at position 34), ABA34-306 and ABA212-306 (the ABA chimeras). Those between aldolases B and C are BC243, BC263 and BC306 (the BC chimeras connected at positions as indicated), as well as CB55, CB243, CB263 and CB306 (the CB chimeras connected at positions as indicated), CBC55-263 (a CBC chimera), and BCB55-193, BCB55-306, BCB79-193 and BCB79-306 (the BCB chimeric enzymes). Through the analysis of the properties of these chimeras, it was found that for aldolase B, isozyme B group-specific sequences (IGSs)-l and-4 were required for exerting type B-specific functions, while the IGSs-2 and -3 enhanced, in collaboration with the IGS-1, the catalytic activity of aldolase B. In addition, the α/β-barrel and the restricted stretches, which were not specified but occupied two distinct regions spanning the amino acid positions 108-137 (designated connector 1) and 243-306 (designated connector 2), were found to be indispensable for showing full catalytic activity of aldolase B.

Original languageEnglish
Pages (from-to)1387-1393
Number of pages7
JournalProtein Engineering, Design and Selection
Volume7
Issue number11
DOIs
Publication statusPublished - Nov 1994
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Bioengineering
  • Biochemistry
  • Molecular Biology

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