VAT‐1 from Torpedo is a membranous homologue of zeta crystallin

FEBS Letters

Linial, Michael¹  Levius, Orit¹ 

[1] Department of Biological Chemistry, The Alexander Silverman Institute of Life Science, The Hebrew University, Jerusalem 91904, Israel

关键词: Electric organ;    Lens crystallin;    Oxidoreductase;    Protein evolution;    Synaptic vesicle;    SDS;    sodium dodecyl sulfate;    PAGE;    polyacrylamidegel electrophoresis;    ADH;    alcohol dehydrogenase;    FAS;    fatty acid ynthase;    aa;    amino acid;   

DOI  :  10.1016/0014-5793(93)81140-U

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

VAT-1 is a major protein from Torpedo synaptic vesicles. A protein data-base search revealed a striking homology to ξ crystallin from guinea pig lens. The overall amino-acid identity is 27%, and 58% similarity is reached by including conserved substitutions. The highest similarity (60% to 85%) between the two proteins is observed in five discrete domains, which are also conserved in zinc-dependent dehydrogenases, particularly in the alcohol dehydrogenase family. The cofactor-binding domain of oxidoreductases is conserved in VAT-1 and in ξ crystallin. VAT-1 preferably binds NADPH in the presence of zinc. In contrast with its homologous proteins, VAT-1 is an integral membrane protein of synaptic vesicles.

【 授权许可】

Unknown