NADP-dependent isopropanol dehydrogenase
Details
- Name
- NADP-dependent isopropanol dehydrogenase
- Synonyms
- 1.1.1.80
- Gene Name
- adh
- Organism
- Thermoanaerobacter brockii
- Amino acid sequence
>lcl|BSEQ0011356|NADP-dependent isopropanol dehydrogenase MKGFAMLSIGKVGWIEKEKPAPGPFDAIVRPLAVAPCTSDIHTVFEGAIGERHNMILGHE AVGEVVEVGSEVKDFKPGDRVVVPAITPDWRTSEVQRGYHQHSGGMLAGWKFSNVKDGVF GEFFHVNDADMNLAHLPKEIPLEAAVMIPDMMTTGFHGAELADIELGATVAVLGIGPVGL MAVAGAKLRGAGRIIAVGSRPVCVDAAKYYGATDIVNYKDGPIESQIMNLTEGKGVDAAI IAGGNADIMATAVKIVKPGGTIANVNYFGEGEVLPVPRLEWGCGMAHKTIKGGLCPGGRL RMERLIDLVFYKRVDPSKLVTHVFRGFDNIEKAFMLMKDKPKDLIKPVVILA
- Number of residues
- 352
- Molecular Weight
- 37646.685
- Theoretical pI
- 6.86
- GO Classification
- Functionsisopropanol dehydrogenase (NADP+) activity / zinc ion binding
- General Function
- Zinc ion binding
- Specific Function
- Alcohol dehydrogenase with a preference for medium chain secondary alcohols, such as 2-butanol and isopropanol. Has very low activity with primary alcohols, such as ethanol. Under physiological conditions, the enzyme reduces aldehydes and 2-ketones to produce secondary alcohols. Is also active with acetaldehyde and propionaldehyde.
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0003747|1059 bp ATGAAAGGTTTTGCAATGCTCAGTATCGGTAAAGTTGGCTGGATTGAGAAGGAAAAGCCT GCTCCTGGCCCATTTGATGCTATTGTAAGACCTCTAGCTGTGGCCCCTTGCACTTCGGAC ATTCATACCGTTTTTGAAGGCGCCATTGGCGAAAGACATAACATGATACTCGGTCACGAA GCTGTAGGTGAAGTAGTTGAAGTAGGTAGTGAGGTAAAAGATTTTAAACCTGGTGATCGC GTTGTTGTGCCAGCTATTACCCCTGATTGGCGGACCTCTGAAGTACAAAGAGGATATCAC CAGCACTCCGGTGGAATGCTGGCAGGCTGGAAATTTTCGAATGTAAAAGATGGTGTTTTT GGTGAATTTTTTCATGTGAATGATGCTGATATGAATTTAGCACATCTGCCTAAAGAAATT CCATTGGAAGCTGCAGTTATGATTCCCGATATGATGACCACTGGTTTTCACGGAGCTGAA CTGGCAGATATAGAATTAGGTGCGACGGTAGCAGTTTTGGGTATTGGCCCAGTAGGTCTT ATGGCAGTCGCTGGTGCCAAATTGCGTGGAGCCGGAAGAATTATTGCCGTAGGCAGTAGA CCAGTTTGTGTAGATGCTGCAAAATACTATGGAGCTACTGATATTGTAAACTATAAAGAT GGTCCTATCGAAAGTCAGATTATGAATCTAACTGAAGGCAAAGGTGTCGATGCTGCCATC ATCGCTGGAGGAAATGCTGACATTATGGCTACAGCAGTTAAGATTGTTAAACCTGGTGGC ACCATCGCTAATGTAAATTATTTTGGCGAAGGAGAGGTTTTGCCTGTTCCTCGTCTTGAA TGGGGTTGCGGCATGGCTCATAAAACTATAAAAGGCGGGCTATGCCCCGGTGGACGTCTA AGAATGGAAAGACTGATTGACCTTGTTTTTTATAAGCGTGTCGATCCTTCTAAGCTCGTC ACTCACGTTTTCCGGGGATTTGACAATATTGAAAAAGCCTTTATGTTGATGAAAGACAAA CCAAAAGACCTAATCAAACCTGTTGTAATATTAGCATAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P14941 UniProtKB Entry Name ADH_THEBR GenBank Protein ID 1771791 GenBank Gene ID X64841 - General References
- Peretz M, Burstein Y: Amino acid sequence of alcohol dehydrogenase from the thermophilic bacterium Thermoanaerobium brockii. Biochemistry. 1989 Aug 8;28(16):6549-55. [Article]
- Korkhin Y, Kalb(Gilboa) AJ, Peretz M, Bogin O, Burstein Y, Frolow F: NADP-dependent bacterial alcohol dehydrogenases: crystal structure, cofactor-binding and cofactor specificity of the ADHs of Clostridium beijerinckii and Thermoanaerobacter brockii. J Mol Biol. 1998 May 22;278(5):967-81. [Article]
- Goihberg E, Peretz M, Tel-Or S, Dym O, Shimon L, Frolow F, Burstein Y: Biochemical and structural properties of chimeras constructed by exchange of cofactor-binding domains in alcohol dehydrogenases from thermophilic and mesophilic microorganisms. Biochemistry. 2010 Mar 9;49(9):1943-53. doi: 10.1021/bi901730x. [Article]