TY - JOUR
T1 - Human aldolase b
T2 - Liver-specific properties of the isozyme depend on type b isozyme group-specific sequences
AU - Kusakabe, Takahiro
AU - Motoki, Kiyohisa
AU - Sugimoto, Yasushi
AU - Takasaki, Yozo
AU - Hori, Katsuji
N1 - Funding Information:
This work was supported in part by a Grant in Aid from the Ministry of Education, Science and Culture of Japan.
PY - 1994/11
Y1 - 1994/11
N2 - 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.
AB - 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.
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U2 - 10.1093/protein/7.11.1387
DO - 10.1093/protein/7.11.1387
M3 - Article
C2 - 7700871
AN - SCOPUS:0028173596
SN - 1741-0126
VL - 7
SP - 1387
EP - 1393
JO - Protein Engineering, Design and Selection
JF - Protein Engineering, Design and Selection
IS - 11
ER -