>lcl|BSEQ0021993|Pentaerythritol tetranitrate reductase
MSAEKLFTPLKVGAVTAPNRVFMAPLTRLRSIEPGDIPTPLMGEYYRQRASAGLIISEAT
QISAQAKGYAGAPGLHSPEQIAAWKKITAGVHAEDGRIAVQLWHTGRISHSSIQPGGQAP
VSASALNANTRTSLRDENGNAIRVDTTTPRALELDEIPGIVNDFRQAVANAREAGFDLVE
LHSAHGYLLHQFLSPSSNQRTDQYGGSVENRARLVLEVVDAVCNEWSADRIGIRVSPIGT
FQNVDNGPNEEADALYLIEELAKRGIAYLHMSETDLAGGKPYSEAFRQKVRERFHGVIIG
AGAYTAEKAEDLIGKGLIDAVAFGRDYIANPDLVARLQKKAELNPQRPESFYGGGAEGYT
DYPSL

>lcl|BSEQ0004906|1098 bp
ATGTCCGCTGAAAAGCTGTTTACCCCACTGAAAGTGGGTGCCGTTACTGCCCCAAACCGC
GTGTTTATGGCCCCACTTACCCGTCTGCGCAGCATCGAGCCGGGCGATATCCCAACGCCA
TTGATGGGTGAGTATTACCGCCAGCGCGCCAGCGCGGGCCTGATTATCTCCGAAGCCACG
CAGATTTCTGCTCAGGCAAAAGGCTACGCCGGTGCACCGGGTCTGCACAGCCCGGAACAG
ATCGCCGCGTGGAAAAAAATCACCGCAGGCGTGCATGCTGAAGATGGCCGTATTGCGGTT
CAGCTGTGGCACACCGGTCGTATCTCACACAGCAGCATCCAGCCTGGCGGTCAGGCGCCG
GTTTCTGCCTCTGCCCTGAACGCCAATACCCGCACTTCCCTGCGCGATGAAAACGGTAAT
GCGATCCGCGTCGACACCACCACGCCACGCGCGCTGGAGCTGGACGAGATCCCGGGTATC
GTGAATGATTTCCGTCAGGCCGTCGCCAACGCCCGGGAAGCGGGCTTCGACCTGGTTGAG
CTTCACTCTGCGCACGGTTACCTGCTGCATCAGTTCCTGTCCCCGTCTTCCAACCAGCGT
ACCGACCAGTACGGCGGCAGCGTTGAAAACCGCGCGCGTCTGGTGCTTGAAGTGGTGGAT
GCTGTCTGTAATGAGTGGAGCGCAGACCGCATTGGTATTCGTGTCTCCCCGATCGGTACT
TTCCAGAACGTCGACAACGGTCCGAACGAAGAAGCAGACGCGCTGTATCTGATTGAAGAG
CTGGCGAAACGCGGTATCGCCTATCTGCACATGTCCGAGACGGACTTGGCAGGCGGCAAG
CCTTACAGTGAAGCCTTCCGTCAGAAAGTGCGCGAGCGCTTCCACGGCGTGATTATCGGG
GCGGGTGCGTATACGGCAGAAAAAGCCGAGGATTTGATCGGTAAAGGCCTGATCGACGCC
GTGGCCTTTGGCCGTGACTACATTGCTAACCCGGATCTGGTTGCCCGTTTGCAGAAAAAA
GCCGAACTGAACCCGCAGCGTCCTGAAAGCTTCTATGGCGGCGGCGCGGAAGGTTATACC
GACTACCCTTCACTGTAA

1. 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. [11428899 ]
2. 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. [11923299 ]
3. 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. [15128738 ]
4. 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. [16156787 ]
5. 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. [19891489 ]
6. 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. [21064170 ]
7. 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. [21374779 ]