The role of zinc for alcohol dehydrogenase structure and function Export

@article{citeulike:3590920, abstract = {Abstract.\ \ Zinc plays an important role in the structure and function of many enzymes, including alcohol dehydrogenases (ADHs) of the MDR type (mediumchain dehydrogenases/reductases). Active site zinc participates in catalytic events, and structural site zinc maintains structural stability. MDR-types of ADHs have both of these zinc sites but with some variation in ligands and spacing. The catalytic zinc sites involve three residues with different spacings from two separate protein segments, while the structural zinc sites involve four residues and cover a local segment of the protein chain (Cys97-Cys111 in horse liver class I ADH). This review summarizes properties of both ADH zinc sites, and relates them to zinc sites of proteins in general. In addition, it highlights a separate study of zinc binding peptide variants of the horse liver ADH structural zinc site. The results show that zinc coordination of the free peptide differs markedly from that of the enzyme (one His / three Cys versus four Cys), suggesting that the protein zinc site is in an energetically strained conformation relative to that of the peptide. This finding is a characteristic of an entatic state, implying a functional nature for this zinc site.}, author = {Auld, D. and Bergman, T.}, citeulike-article-id = {3590920}, citeulike-linkout-0 = {http://dx.doi.org/10.1007/s00018-008-8593-1}, citeulike-linkout-1 = {http://www.springerlink.com/content/f2614862182k3128}, doi = {10.1007/s00018-008-8593-1}, journal = {Cellular and Molecular Life Sciences (CMLS)}, posted-at = {2009-03-26 02:25:32}, priority = {2}, title = {The role of zinc for alcohol dehydrogenase structure and function}, url = {http://dx.doi.org/10.1007/s00018-008-8593-1} }

TY - JOUR ID - citeulike:3590920 L3 - citeulike-article-id:3590920 N2 - Abstract.  Zinc plays an important role in the structure and function of many enzymes, including alcohol dehydrogenases (ADHs) of the MDR type (mediumchain dehydrogenases/reductases). Active site zinc participates in catalytic events, and structural site zinc maintains structural stability. MDR-types of ADHs have both of these zinc sites but with some variation in ligands and spacing. The catalytic zinc sites involve three residues with different spacings from two separate protein segments, while the structural zinc sites involve four residues and cover a local segment of the protein chain (Cys97-Cys111 in horse liver class I ADH). This review summarizes properties of both ADH zinc sites, and relates them to zinc sites of proteins in general. In addition, it highlights a separate study of zinc binding peptide variants of the horse liver ADH structural zinc site. The results show that zinc coordination of the free peptide differs markedly from that of the enzyme (one His / three Cys versus four Cys), suggesting that the protein zinc site is in an energetically strained conformation relative to that of the peptide. This finding is a characteristic of an entatic state, implying a functional nature for this zinc site. JF - Cellular and Molecular Life Sciences (CMLS) TI - The role of zinc for alcohol dehydrogenase structure and function AU - Auld, D AU - Bergman, T UR - http://dx.doi.org/10.1007/s00018-008-8593-1 ER -