Abstract:
:To study the structure/function relationship and enzymatic properties of human aldolase C, we have constructed an Escherichia coli expression plasmid, pHAC11, for the isozyme. E. coli cells carrying this plasmid produced enzymatically active human aldolase C. The kcat and Km values for fructose-1,6-bisphosphate (Fru-1,6-P2) and fructose-1-phosphate (Fru-1-P) of the recombinant enzyme were found to be similar to those of authentic aldolase C from human brain. The Fru-1,6-P2/Fru-1-P activity ratio of the recombinant enzyme is approximately 13.5, which is comparable to that of the recombinant rat aldolase C, but is slightly higher than those of rat brain and hepatoma aldolases C. The substitution of Ser for the carboxyl-terminal Tyr (Tyr-363) of the recombinant enzyme caused a marked decrease in that of Fru-1,6-P2, with little change in that of Fru-1-P. The activity ratio changed from 13.5 for the normal enzyme to 3.8 for the engineered enzyme. Human aldolase C was found to form tetrameric hybrids with aldolase B in vivo when these enzymes were coexpressed in E. coli cells.
journal_name
J Biochemjournal_title
Journal of biochemistryauthors
Kusakabe T,Motoki K,Hori Kdoi
10.1093/oxfordjournals.jbchem.a124475subject
Has Abstractpub_date
1994-06-01 00:00:00pages
1172-7issue
6eissn
0021-924Xissn
1756-2651journal_volume
115pub_type
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pub_type: 杂志文章
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pub_type: 杂志文章
doi:10.1093/oxfordjournals.jbchem.a122783
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pub_type: 杂志文章
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doi:10.1093/oxfordjournals.jbchem.a123176
更新日期:1990-08-01 00:00:00
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doi:10.1093/oxfordjournals.jbchem.a022508
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pub_type: 杂志文章
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doi:
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