Stopped-Flow Studies of Human Aldose Reductase Reveal which Enzyme form Predominates During Steady-State Turnover in Either Reaction Direction View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

1995

AUTHORS

Charles E. Grimshaw , Chung-Jeng Lai

ABSTRACT

Progress in the aldo-keto reductase field has been quite rapid since the solution of the 3-dimensional structure of aldose reductase (ALR2) by the French group (Rondeau et al., 1992) and the Baylor group (Wilson et al., 1992), with additional contributions from Washington University School of Medicine with BioCryst Pharmaceuticals (Borhani et al., 1992) and with Dr. Quiocho’s laboratory (Wilson et al., 1993). Most recently, a definitive assignment of the active site constellation of amino acid residues and their likely roles in the catalytic mechanism was established by the collaborative efforts of researchers at Baylor, Brandeis and The Whittier Institute (Harrison et al., 1994; Bohren et al., 1994). More... »

PAGES

229-40

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4615-1965-2_29

DOI

http://dx.doi.org/10.1007/978-1-4615-1965-2_29

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1006228017

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7484383


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