Parathion hydrolase
Details
- Name
- Parathion hydrolase
- Synonyms
- 3.1.8.1
- Phosphotriesterase
- PTE
- Gene Name
- opd
- Organism
- Brevundimonas diminuta
- Amino acid sequence
>lcl|BSEQ0007716|Parathion hydrolase MQTRRVVLKSAAAAGTLLGGLAGCASVAGSIGTGDRINTVRGPITISEAGFTLTHEHICG SSAGFLRAWPEFFGSRKALAEKAVRGLRRARAAGVRTIVDVSTFDIGRDVSLLAEVSRAA DVHIVAATGLWFDPPLSMRLRSVEELTQFFLREIQYGIEDTGIRAGIIKVATTGKATPFQ ELVLKAAARASLATGVPVTTHTAASQRDGEQQAAIFESEGLSPSRVCIGHSDDTDDLSYL TALAARGYLIGLDHIPHSAIGLEDNASASALLGIRSWQTRALLIKALIDQGYMKQILVSN DWLFGFSSYVTNIMDVMDRVNPDGMAFIPLRVIPFLREKGVPQETLAGITVTNPARFLSP TLRAS
- Number of residues
- 365
- Molecular Weight
- 39003.24
- Theoretical pI
- 8.48
- GO Classification
- Functionsaryldialkylphosphatase activity / zinc ion bindingProcessescatabolic processComponentsplasma membrane
- General Function
- Has an unusual substrate specificity for synthetic organophosphate triesters and phosphorofluoridates. All of the phosphate triesters found to be substrates are synthetic compounds. The identity of any naturally occurring substrate for the enzyme is unknown. Has no detectable activity with phosphate monoesters or diesters and no activity as an esterase or protease. It catalyzes the hydrolysis of the insecticide paraoxon at a rate approaching the diffusion limit and thus appears to be optimally evolved for utilizing this synthetic substrate.
- Specific Function
- Aryldialkylphosphatase activity
- Pfam Domain Function
- PTE (PF02126)
- Transmembrane Regions
- Not Available
- Cellular Location
- Cell membrane
- Gene sequence
>lcl|BSEQ0007715|978 bp GTAAGCAATCGCAAGGGGGCAGCATGCAAACGAGAAGGGTTGTGCTCAAGTCTGCGGCCG CGAGAACTCTGCTCGGCGGCCTGGCTGGGTGCGCGACGTGGCTGGATCGATCGGCACAGG CGATGCGATCAATACGTGCGCGTCCTATCACAATCTCTGAAGCGGGTTTCACACTGACTC ACGAGGACATCTCGGCAGCTCGGCAGGATTCTTGCGTGCTTGGCCAGAGTTCTTCGGTAG CGCAAAGCTCTAGCGGAAAAGGCTGTGAGAGGATTGCGCGCCAGAGCGGCTGGCGTGCGA ACGATTGTCGATGTGTCGACTTTCGATATCGGTCGCGACGTCAGTTTATTGGCCGAGGTT TCGCGGGCTGCCGACGTTCATATCTGGCGGCGACCGGCTTGTGGTTCGACCCGCCACTTT CGATGCGATTGAGGTATGTAGAGGAACTCACACTAGTTCTTCCTGCGGTGAGATTCAATA TGGCATCGAAGTACACCGGAATTAGGGCGGGCATTATCAAGGTCGCGACCACAGGCAAGG CGACCCCCTTTCAGGAGTTAGTGTTAAAGGCGGCCGCCCGGGCCAGCTTGGCCACCGGTG TTCCGGTAACCACTCACACGGCAGCAAGTCAGCGCGATGGTGAGCGAGGCAGGCCGCCAT TTTTGAGTCCGAAGCTTGAGCCCTCACGGGTTTGTATTGGTCACAGCGATGATACTGACG ATTTGAGCTATCTCACCGCCCTGCTGCGCGGATACCTCATCGGTCTAGACCACATCCCGC ACAGTGCGATTGGTCTAGAAGATAATGCGAGTGCATCACCGCTCCTGGGCATCCGTTCGT GGCAAACACGGGCTCTCTTGATCAAGGCGCTCATCGACCAAGGCTACATGAAACAAATCC TCGTTTCGAATGACTGGCTGTTCGGGTTTTCGAGCTATGTCACCAACATCATGGACGTGA TGGATCGCGTGAACCCCG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A434 UniProtKB Entry Name OPD_BREDI GenBank Protein ID 151518 GenBank Gene ID M20392 - General References
- McDaniel CS, Harper LL, Wild JR: Cloning and sequencing of a plasmid-borne gene (opd) encoding a phosphotriesterase. J Bacteriol. 1988 May;170(5):2306-11. [Article]
- Kuo JM, Raushel FM: Identification of the histidine ligands to the binuclear metal center of phosphotriesterase by site-directed mutagenesis. Biochemistry. 1994 Apr 12;33(14):4265-72. [Article]
- Benning MM, Kuo JM, Raushel FM, Holden HM: Three-dimensional structure of phosphotriesterase: an enzyme capable of detoxifying organophosphate nerve agents. Biochemistry. 1994 Dec 20;33(50):15001-7. [Article]
- Benning MM, Kuo JM, Raushel FM, Holden HM: Three-dimensional structure of the binuclear metal center of phosphotriesterase. Biochemistry. 1995 Jun 27;34(25):7973-8. [Article]
- Vanhooke JL, Benning MM, Raushel FM, Holden HM: Three-dimensional structure of the zinc-containing phosphotriesterase with the bound substrate analog diethyl 4-methylbenzylphosphonate. Biochemistry. 1996 May 14;35(19):6020-5. [Article]