Oxygen-insensitive NAD(P)H nitroreductase
Details
- Name
- Oxygen-insensitive NAD(P)H nitroreductase
- Synonyms
- 1.-.-.-
- Dihydropteridine reductase
- dprA
- FMN-dependent nitroreductase
- nfnB
- nfsI
- ntr
- Gene Name
- nfsB
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0019145|Oxygen-insensitive NAD(P)H nitroreductase MDIISVALKRHSTKAFDASKKLTPEQAEQIKTLLQYSPSSTNSQPWHFIVASTEEGKARV AKSAAGNYVFNERKMLDASHVVVFCAKTAMDDVWLKLVVDQEDADGRFATPEAKAANDKG RKFFADMHRKDLHDDAEWMAKQVYLNVGNFLLGVAALGLDAVPIEGFDAAILDAEFGLKE KGYTSLVVVPVGHHSVEDFNATLPKSRLPQNITLTEV
- Number of residues
- 217
- Molecular Weight
- 23904.99
- Theoretical pI
- 6.16
- GO Classification
- Functions6,7-dihydropteridine reductase activity / FMN binding / identical protein binding / NAD(P)H nitroreductase activityProcesses2,4,6-trinitrotoluene catabolic processComponentscytosol / membrane
- General Function
- Nad(p)h nitroreductase activity
- Specific Function
- Reduction of a variety of nitroaromatic compounds using NADH (and to lesser extent NADPH) as source of reducing equivalents; two electrons are transferred. Capable of reducing nitrofurazone, quinones and the anti-tumor agent CB1954 (5-(aziridin-1-yl)-2,4-dinitrobenzamide). The reduction of CB1954 results in the generation of cytotoxic species.
- Pfam Domain Function
- Nitroreductase (PF00881)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0019146|Oxygen-insensitive NAD(P)H nitroreductase (nfsB) ATGGATATCATTTCTGTCGCCTTAAAGCGTCATTCCACTAAGGCATTTGATGCCAGCAAA AAACTTACCCCGGAACAGGCCGAGCAGATCAAAACGCTACTGCAATACAGCCCATCCAGC ACCAACTCCCAGCCGTGGCATTTTATTGTTGCCAGCACGGAAGAAGGTAAAGCGCGTGTT GCCAAATCCGCTGCCGGTAATTACGTGTTCAACGAGCGTAAAATGCTTGATGCCTCGCAC GTCGTGGTGTTCTGTGCAAAAACCGCGATGGACGATGTCTGGCTGAAGCTGGTTGTTGAC CAGGAAGATGCCGATGGCCGCTTTGCCACGCCGGAAGCGAAAGCCGCGAACGATAAAGGT CGCAAGTTCTTCGCTGATATGCACCGTAAAGATCTGCATGATGATGCAGAGTGGATGGCA AAACAGGTTTATCTCAACGTCGGTAACTTCCTGCTCGGCGTGGCGGCTCTGGGTCTGGAC GCGGTACCCATCGAAGGTTTTGACGCCGCCATCCTCGATGCAGAATTTGGTCTGAAAGAG AAAGGCTACACCAGTCTGGTGGTTGTTCCGGTAGGTCATCACAGCGTTGAAGATTTTAAC GCTACGCTGCCGAAATCTCGTCTGCCGCAAAACATCACCTTAACCGAAGTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P38489 UniProtKB Entry Name NFSB_ECOLI GenBank Protein ID 538227 GenBank Gene ID D25414 - General References
- Zenno S, Koike H, Tanokura M, Saigo K: Gene cloning, purification, and characterization of NfsB, a minor oxygen-insensitive nitroreductase from Escherichia coli, similar in biochemical properties to FRase I, the major flavin reductase in Vibrio fischeri. J Biochem. 1996 Oct;120(4):736-44. [Article]
- Michael NP, Brehm JK, Anlezark GM, Minton NP: Physical characterisation of the Escherichia coli B gene encoding nitroreductase and its over-expression in Escherichia coli K12. FEMS Microbiol Lett. 1994 Dec 1;124(2):195-202. [Article]
- Oshima T, Aiba H, Baba T, Fujita K, Hayashi K, Honjo A, Ikemoto K, Inada T, Itoh T, Kajihara M, Kanai K, Kashimoto K, Kimura S, Kitagawa M, Makino K, Masuda S, Miki T, Mizobuchi K, Mori H, Motomura K, Nakamura Y, Nashimoto H, Nishio Y, Saito N, Horiuchi T, et al.: A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map. DNA Res. 1996 Jun 30;3(3):137-55. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Anlezark GM, Melton RG, Sherwood RF, Coles B, Friedlos F, Knox RJ: The bioactivation of 5-(aziridin-1-yl)-2,4-dinitrobenzamide (CB1954)--I. Purification and properties of a nitroreductase enzyme from Escherichia coli--a potential enzyme for antibody-directed enzyme prodrug therapy (ADEPT). Biochem Pharmacol. 1992 Dec 15;44(12):2289-95. [Article]
- Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
- Vasudevan SG, Shaw DC, Armarego WL: Dihydropteridine reductase from Escherichia coli. Biochem J. 1988 Oct 15;255(2):581-8. [Article]
- Parkinson GN, Skelly JV, Neidle S: Crystal structure of FMN-dependent nitroreductase from Escherichia coli B: a prodrug-activating enzyme. J Med Chem. 2000 Oct 5;43(20):3624-31. [Article]
- Lovering AL, Hyde EI, Searle PF, White SA: The structure of Escherichia coli nitroreductase complexed with nicotinic acid: three crystal forms at 1.7 A, 1.8 A and 2.4 A resolution. J Mol Biol. 2001 May 25;309(1):203-13. [Article]
- Johansson E, Parkinson GN, Denny WA, Neidle S: Studies on the nitroreductase prodrug-activating system. Crystal structures of complexes with the inhibitor dicoumarol and dinitrobenzamide prodrugs and of the enzyme active form. J Med Chem. 2003 Sep 11;46(19):4009-20. [Article]
- Race PR, Lovering AL, Green RM, Ossor A, White SA, Searle PF, Wrighton CJ, Hyde EI: Structural and mechanistic studies of Escherichia coli nitroreductase with the antibiotic nitrofurazone. Reversed binding orientations in different redox states of the enzyme. J Biol Chem. 2005 Apr 8;280(14):13256-64. Epub 2005 Jan 31. [Article]
Drug Relations
- Drug Relations
DrugBank ID Name Drug group Pharmacological action? Actions Details DB03228 5-[Bis-2(Chloro-Ethyl)-Amino]-2,4-Dintro-Benzamide experimental unknown Details DB03247 Flavin mononucleotide approved, investigational unknown Details DB04138 5-[Bis(2-bromoethyl)amino]-N-(2,3-dioxopropyl)-2,4-dinitrobenzamide experimental unknown Details DB04253 Tretazicar investigational unknown Details DB04392 Bishydroxy[2h-1-Benzopyran-2-One,1,2-Benzopyrone] experimental unknown Details