THE CALCIUM BINDING SITES OF THE BAKERS' YEAST TRANSKETOLASE
The calcium binding sites of Bakers' Yeast Transketolase (TK) was elucidated by estimating the pKa values of the functional groups that bind to calcium. These pKa's were found to be 6.25 and 7.2 relating to the pKa's of the two immidazol moieties of histidine residues on the enzyme. T...
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| Format: | Article |
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| Language: | English |
| Published: |
University of Tehran
1992-12-01
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| Series: | Journal of Sciences, Islamic Republic of Iran |
| Online Access: | https://jsciences.ut.ac.ir/article_31510_82d72ee698f4df1e406a40a936bda38e.pdf |
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| collection | DOAJ |
| description | The calcium binding sites of Bakers' Yeast Transketolase (TK) was elucidated
by estimating the pKa values of the functional groups that bind to calcium. These
pKa's were found to be 6.25 and 7.2 relating to the pKa's of the two immidazol
moieties of histidine residues on the enzyme. The rate of the binding of calcium to
the enzyme was obtained separately as a function of pH. Maximum values were
obtained at the pKa's of the immidazol rings of histidine correlating closely with the
values obtained by direct titration. The activity rate studies as a function of pH
showed that the enzyme, when bound to its cofactors, becomes further activated
over and above the regular increasing trend of the pH rate profile at similar pH's
which are optimal for calcium binding |
| format | Article |
| id | doaj-art-e3e37f1f90374ac691c0d608815c19da |
| institution | OA Journals |
| issn | 1016-1104 2345-6914 |
| language | English |
| publishDate | 1992-12-01 |
| publisher | University of Tehran |
| record_format | Article |
| series | Journal of Sciences, Islamic Republic of Iran |
| spelling | doaj-art-e3e37f1f90374ac691c0d608815c19da2025-08-20T02:25:51ZengUniversity of TehranJournal of Sciences, Islamic Republic of Iran1016-11042345-69141992-12-013231510THE CALCIUM BINDING SITES OF THE BAKERS' YEAST TRANSKETOLASEThe calcium binding sites of Bakers' Yeast Transketolase (TK) was elucidated by estimating the pKa values of the functional groups that bind to calcium. These pKa's were found to be 6.25 and 7.2 relating to the pKa's of the two immidazol moieties of histidine residues on the enzyme. The rate of the binding of calcium to the enzyme was obtained separately as a function of pH. Maximum values were obtained at the pKa's of the immidazol rings of histidine correlating closely with the values obtained by direct titration. The activity rate studies as a function of pH showed that the enzyme, when bound to its cofactors, becomes further activated over and above the regular increasing trend of the pH rate profile at similar pH's which are optimal for calcium bindinghttps://jsciences.ut.ac.ir/article_31510_82d72ee698f4df1e406a40a936bda38e.pdf |
| spellingShingle | THE CALCIUM BINDING SITES OF THE
BAKERS' YEAST TRANSKETOLASE Journal of Sciences, Islamic Republic of Iran |
| title | THE CALCIUM BINDING SITES OF THE
BAKERS' YEAST TRANSKETOLASE |
| title_full | THE CALCIUM BINDING SITES OF THE
BAKERS' YEAST TRANSKETOLASE |
| title_fullStr | THE CALCIUM BINDING SITES OF THE
BAKERS' YEAST TRANSKETOLASE |
| title_full_unstemmed | THE CALCIUM BINDING SITES OF THE
BAKERS' YEAST TRANSKETOLASE |
| title_short | THE CALCIUM BINDING SITES OF THE
BAKERS' YEAST TRANSKETOLASE |
| title_sort | calcium binding sites of the bakers yeast transketolase |
| url | https://jsciences.ut.ac.ir/article_31510_82d72ee698f4df1e406a40a936bda38e.pdf |