Pentaerythritol tetranitrate reductase
Details
- Name
- Pentaerythritol tetranitrate reductase
- Synonyms
- Not Available
- Gene Name
- onr
- Organism
- Enterobacter cloacae
- Amino acid sequence
>lcl|BSEQ0021993|Pentaerythritol tetranitrate reductase MSAEKLFTPLKVGAVTAPNRVFMAPLTRLRSIEPGDIPTPLMGEYYRQRASAGLIISEAT QISAQAKGYAGAPGLHSPEQIAAWKKITAGVHAEDGRIAVQLWHTGRISHSSIQPGGQAP VSASALNANTRTSLRDENGNAIRVDTTTPRALELDEIPGIVNDFRQAVANAREAGFDLVE LHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAVCNEWSADRIGIRVSPIGT FQNVDNGPNEEADALYLIEELAKRGIAYLHMSETDLAGGKPYSEAFRQKVRERFHGVIIG AGAYTAEKAEDLIGKGLIDAVAFGRDYIANPDLVARLQKKAELNPQRPESFYGGGAEGYT DYPSL
- Number of residues
- 365
- Molecular Weight
- 39488.93
- Theoretical pI
- 6.06
- GO Classification
- FunctionsFMN binding / oxidoreductase activity
- General Function
- Oxidoreductase activity
- Specific Function
- Not Available
- Pfam Domain Function
- Oxidored_FMN (PF00724)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0004906|1098 bp ATGTCCGCTGAAAAGCTGTTTACCCCACTGAAAGTGGGTGCCGTTACTGCCCCAAACCGC GTGTTTATGGCCCCACTTACCCGTCTGCGCAGCATCGAGCCGGGCGATATCCCAACGCCA TTGATGGGTGAGTATTACCGCCAGCGCGCCAGCGCGGGCCTGATTATCTCCGAAGCCACG CAGATTTCTGCTCAGGCAAAAGGCTACGCCGGTGCACCGGGTCTGCACAGCCCGGAACAG ATCGCCGCGTGGAAAAAAATCACCGCAGGCGTGCATGCTGAAGATGGCCGTATTGCGGTT CAGCTGTGGCACACCGGTCGTATCTCACACAGCAGCATCCAGCCTGGCGGTCAGGCGCCG GTTTCTGCCTCTGCCCTGAACGCCAATACCCGCACTTCCCTGCGCGATGAAAACGGTAAT GCGATCCGCGTCGACACCACCACGCCACGCGCGCTGGAGCTGGACGAGATCCCGGGTATC GTGAATGATTTCCGTCAGGCCGTCGCCAACGCCCGGGAAGCGGGCTTCGACCTGGTTGAG CTTCACTCTGCGCACGGTTACCTGCTGCATCAGTTCCTGTCCCCGTCTTCCAACCAGCGT ACCGACCAGTACGGCGGCAGCGTTGAAAACCGCGCGCGTCTGGTGCTTGAAGTGGTGGAT GCTGTCTGTAATGAGTGGAGCGCAGACCGCATTGGTATTCGTGTCTCCCCGATCGGTACT TTCCAGAACGTCGACAACGGTCCGAACGAAGAAGCAGACGCGCTGTATCTGATTGAAGAG CTGGCGAAACGCGGTATCGCCTATCTGCACATGTCCGAGACGGACTTGGCAGGCGGCAAG CCTTACAGTGAAGCCTTCCGTCAGAAAGTGCGCGAGCGCTTCCACGGCGTGATTATCGGG GCGGGTGCGTATACGGCAGAAAAAGCCGAGGATTTGATCGGTAAAGGCCTGATCGACGCC GTGGCCTTTGGCCGTGACTACATTGCTAACCCGGATCTGGTTGCCCGTTTGCAGAAAAAA GCCGAACTGAACCCGCAGCGTCCTGAAAGCTTCTATGGCGGCGGCGCGGAAGGTTATACC GACTACCCTTCACTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P71278 UniProtKB Entry Name P71278_ENTCL GenBank Gene ID U68759 - General References
- Barna TM, Khan H, Bruce NC, Barsukov I, Scrutton NS, Moody PC: Crystal structure of pentaerythritol tetranitrate reductase: "flipped" binding geometries for steroid substrates in different redox states of the enzyme. J Mol Biol. 2001 Jul 6;310(2):433-47. [Article]
- Khan H, Harris RJ, Barna T, Craig DH, Bruce NC, Munro AW, Moody PC, Scrutton NS: Kinetic and structural basis of reactivity of pentaerythritol tetranitrate reductase with NADPH, 2-cyclohexenone, nitroesters, and nitroaromatic explosives. J Biol Chem. 2002 Jun 14;277(24):21906-12. Epub 2002 Mar 28. [Article]
- Khan H, Barna T, Harris RJ, Bruce NC, Barsukov I, Munro AW, Moody PC, Scrutton NS: Atomic resolution structures and solution behavior of enzyme-substrate complexes of Enterobacter cloacae PB2 pentaerythritol tetranitrate reductase. Multiple conformational states and implications for the mechanism of nitroaromatic explosive degradation. J Biol Chem. 2004 Jul 16;279(29):30563-72. Epub 2004 May 5. [Article]
- Khan H, Barna T, Bruce NC, Munro AW, Leys D, Scrutton NS: Proton transfer in the oxidative half-reaction of pentaerythritol tetranitrate reductase. Structure of the reduced enzyme-progesterone complex and the roles of residues Tyr186, His181, His184. FEBS J. 2005 Sep;272(18):4660-71. [Article]
- Pudney CR, Hay S, Levy C, Pang J, Sutcliffe MJ, Leys D, Scrutton NS: Evidence to support the hypothesis that promoting vibrations enhance the rate of an enzyme catalyzed H-tunneling reaction. J Am Chem Soc. 2009 Dec 2;131(47):17072-3. doi: 10.1021/ja908469m. [Article]
- Hulley ME, Toogood HS, Fryszkowska A, Mansell D, Stephens GM, Gardiner JM, Scrutton NS: Focused directed evolution of pentaerythritol tetranitrate reductase by using automated anaerobic kinetic screening of site-saturated libraries. Chembiochem. 2010 Nov 22;11(17):2433-47. doi: 10.1002/cbic.201000527. [Article]
- Toogood HS, Fryszkowska A, Hulley M, Sakuma M, Mansell D, Stephens GM, Gardiner JM, Scrutton NS: A site-saturated mutagenesis study of pentaerythritol tetranitrate reductase reveals that residues 181 and 184 influence ligand binding, stereochemistry and reactivity. Chembiochem. 2011 Mar 21;12(5):738-49. doi: 10.1002/cbic.201000662. Epub 2011 Mar 4. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB01676 Trinitrotoluene experimental unknown Details DB02060 Cyclohexanone experimental unknown Details DB03247 Flavin mononucleotide approved, investigational unknown Details DB03651 Picric acid experimental unknown Details DB04528 2,4-Dinitrophenol experimental unknown Details DB07373 Boldione experimental unknown Details DB02508 Isopentyl Pyrophosphate experimental unknown Details DB11090 Potassium nitrate approved unknown substrate Details