Role of isozyme group-specific sequence 4 in the isozyme-specific properties of human aldolase C

Takahiro Kusakabe, Kiyohisa Motoki, Yasushi Sugimoto, Katsuji Hori

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To assess which regions of the aldolase C molecule are required for exhibiting isozyme-specific kinetic properties, we have constructed nine chimeric enzymes of human aldolases A and C. Kinetic studies of these chimeric enzymes revealed that aldolase C absolutely required its own isozyme group-specific sequences (IGS), particularly IGS-4, for exhibiting the characteristics of aldolase C which differ significantly from those of isozymes A and B (Kusakabe T, Motoki K, Hori K. Human aldolase C: characterization of the recombinant enzyme expressed in Escherichia coli. J Biochem (Tokyo) 1994;115:1172-7). Whereas human aldolases A and B required their own isozyme group-specific sequences-1 and -4 (IGS-1 and -4) as the main determinants of isozyme-specific kinetic properties (Motoki K, Kitajima Y, Hori K. Isozyme-specific modules on human aldolase A molecule. J Biol Chem 1993;268:1677-83; Kusakabe T, Motoki K, Sugimoto Y, Takasaki Y, Hori K. Human aldolase B: liver-specific properties of the isoenzyme depend on type B isozyme group-specific sequence. Prot. Eng. 1994;7:1387-93), the present studies indicate that the IGS-1 is principally substitutable between aldolases A and C. The kinetic data also suggests that the connector-2 (amino acid residues 243-306) may modulate the interaction of IGS units with the α/β barrel of the aldolase molecule. Copyright (C) 1998 Elsevier Science Inc.

Original languageEnglish
Pages (from-to)665-673
Number of pages9
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Issue number4
Publication statusPublished - 1998

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Physiology
  • Molecular Biology


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