Abstract

Interconversion of alcohols, aldehydes, and ketones are essential processes in both prokaryotes and eukaryotes. The oxidoreductases catalyzing these reactions use a variety of different electron acceptors and can be divided into three main groups: 1. the NAD(P)-dependent alcohol dehydrogenases 2. the NAD(P)-independent alcohol dehydrogenases, which use other cofactors for catalysis; and 3. FAD-dependent alcohol oxidases, which catalyze irreversible oxidation of alcohols. H Thermoanaerobacter (formerly Thermoanaerobium) brockii alcohol Hdehydrogenase (TBADH) is a medium chain, NADP-linked, class A enzyme Hthat reversibly catalyses the oxidation of secondary alcohols to the Hcorresponding ketones. H The ubiquitous alcohol dehydrogenases (ADHs) are found not only Hin bacteria, but also in yeast, plants, insects and in man. ADH is an oxidoreductase, requiring either NAD(H) or NADP(H) as a coenzyme, that reacts with primary and secondary, linear and branched-chain, aliphatic and aromatic alcohols and with their corresponding aldehydes and ketones. Although some ADHs depend on iron for activation and certain ADHs are known to be metal-free, most ADHs contain zinc at the Hactive site. Zinc-dependent ADHs are either dimers, usually found in Hhigher plants and mammals, or tetramers, such as those present in Hyeast and bacteria. A monomeric ADH was isolated from Saccharomyces Hcerevisiae, but its metal content is yet unknown.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Center for Research Resources (NCRR)
Type
Biotechnology Resource Grants (P41)
Project #
2P41RR001633-16
Application #
6120388
Study Section
Project Start
1998-09-30
Project End
1999-08-31
Budget Start
Budget End
Support Year
16
Fiscal Year
1998
Total Cost
Indirect Cost

  Institution

Name
Albert Einstein College of Medicine
Department
Type
DUNS #
009095365
City
Bronx
State
NY
Country
United States
Zip Code
10461

  Publications

Vongsvivut, Jitraporn; Fernandez, Jason; Ekgasit, Sanong et al. (2004) Characterization of supported cylinder-planar germanium waveguide sensors with synchrotron infrared radiation. Appl Spectrosc 58:143-51
Masip, Lluis; Pan, Jonathan L; Haldar, Suranjana et al. (2004) An engineered pathway for the formation of protein disulfide bonds. Science 303:1185-9
Huang, Raymond Y; Miller, Lisa M; Carlson, Cathy S et al. (2003) In situ chemistry of osteoporosis revealed by synchrotron infrared microspectroscopy. Bone 33:514-21
Rashidzadeh, Hassan; Khrapunov, Sergei; Chance, Mark R et al. (2003) Solution structure and interdomain interactions of the Saccharomyces cerevisiae ""TATA binding protein"" (TBP) probed by radiolytic protein footprinting. Biochemistry 42:3655-65
Uchida, Takeshi; Takamoto, Keiji; He, Qin et al. (2003) Multiple monovalent ion-dependent pathways for the folding of the L-21 Tetrahymena thermophila ribozyme. J Mol Biol 328:463-78
Taylor, Colleen M; Watton, Stephen P; Bryngelson, Peter A et al. (2003) Inner-sphere complexation of cobalt(II) 2,9-dimethyl-1,10-phenanthroline ([Co(neo)]2+) with commercial and sol-gel derived silica gel surfaces. Inorg Chem 42:312-20
Dewan, John C; Feeling-Taylor, Angela; Puius, Yoram A et al. (2002) Structure of mutant human carbonmonoxyhemoglobin C (betaE6K) at 2.0 A resolution. Acta Crystallogr D Biol Crystallogr 58:2038-42
Kiselar, J G; Maleknia, S D; Sullivan, M et al. (2002) Hydroxyl radical probe of protein surfaces using synchrotron X-ray radiolysis and mass spectrometry. Int J Radiat Biol 78:101-14
Swisher, Jennifer F; Su, Linhui J; Brenowitz, Michael et al. (2002) Productive folding to the native state by a group II intron ribozyme. J Mol Biol 315:297-310
Dhavan, Gauri M; Crothers, Donald M; Chance, Mark R et al. (2002) Concerted binding and bending of DNA by Escherichia coli integration host factor. J Mol Biol 315:1027-37

Showing the most recent 10 out of 68 publications