The enzymic cleavage of the carbon-phosphorus bond: Purification and properties of phosphonatase

Nauze, Julia M. La; Rosenberg, H.; Shaw, Douglas J.

doi:10.1016/0005-2744(70)90214-7

Cited by 115 publications

(77 citation statements)

References 54 publications

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“…The third P-C bond-cleaving enzyme, phosphonoacetaldehyde hydrolase (trivial name, phosphonatase) (16,17), is the topic of this paper. Phosphonatase serves to mediate the second step of the catabolism of 2-aminoethyl phosphonate (AEP) 1 (Scheme 1) (18,19), the most ubiquitous and abundant of the naturally occurring phosphonates (1).…”

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Insights into the Mechanism of Catalysis by the P−C Bond-Cleaving Enzyme Phosphonoacetaldehyde Hydrolase Derived from Gene Sequence Analysis and Mutagenesis

et al. 1998

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Phosphonoacetaldehyde hydrolase (phosphonatase) catalyzes the hydrolysis of phosphonoacetaldehyde to acetaldehyde and inorganic phosphate. In this study, the genes encoding phosphonatase in Bacillus cereus and in Salmonella typhimurium were cloned for high-level expression in Escherichia coli. The kinetic properties of the purified, recombinant phosphonatases were determined. The Schiff base mechanism known to operate in the B. cereus enzyme was verified for the S. typhimurium enzyme by phosphonoacetaldehyde-sodium borohydride-induced inactivation and by site-directed mutagenesis of the catalytic lysine 53. The protein sequence inferred from the B. cereus phosphonatase gene was determined, and this sequence was used along with that from the S. typhimurium phosphonatase gene sequence to search the primary sequence databases for possible structural homologues. We found that phosphonatase belongs to a novel family of hydrolases which appear to use a highly conserved active site aspartate residue in covalent catalysis. On the basis of this finding and the known stereochemical course of phosphonatase-catalyzed hydrolysis at phosphorus (retention), we propose a mechanism which involves Schiff base formation with lysine 53 followed by phosphoryl transfer to aspartate (at position 11 in the S. typhimurium enzyme and position 12 in the B. cereus phosphonatase) and last hydrolysis at the imine C(1) and acyl phosphate phosphorus.Phosphonates constitute a class of naturally occurring organophosphorus compounds which differ in structure from the more predominate phosphate esters by the direct linkage of phosphorus to carbon (1-3). The P-C bond is resistant to acid-and base-catalyzed hydrolysis as well as to enzymes which catalyze the cleavage of P-O-C bonds in phosphate esters. Their similarity to phosphate ester structure, coupled with their stability, gives phosphonates a variety of biological properties which we have seen exploited in both natural products (e.g., antibiotics and phosphatase-resistant membrane components) and synthetics (e.g., insecticides, herbicides, and pharmaceuticals). Although phosphonates have been found in numerous organisms ranging from bacteria to mammals, active synthesis of phosphonates has thus far been demonstrated in only certain bacteria (4-6), a protozoan Tetrahymena pyriformis (7,8), and a mollusk Mytilus edulis (9). Phosphonate degradative pathways, on the other hand, have been demonstrated only in bacteria (1-3).It has been speculated that phosphonate natural products are a vestige of an earlier era on earth when reduced forms of organophosphorus compounds predominated over organophosphates (1-3, 10). If this is true, then the phosphonohydrolases are likely to have evolved long ago to allow the cycling of phosphorus between phosphonates and phosphates. Presently, three P-C bond-cleaving enzymes are known. The C-P lyase, which has a very broad substrate specificity, cleaves the C-P bond homolytically, yet ultimately produces inorganic phosphate and the corresponding hydrocarbon...

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Insights into the Mechanism of Catalysis by the P−C Bond-Cleaving Enzyme Phosphonoacetaldehyde Hydrolase Derived from Gene Sequence Analysis and Mutagenesis

et al. 1998

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“…Furthermore, "phosphonatase" was shown to be inactive on alkyl-and phenylphosphonic acids. 14 ) Therefore, the C-P bond cleavage enzyme we found in E. aerogenes IFO 12010 is different from "phosphonatase," although the occurrence of the latter enzyme has not been confirmed in E. aerogenes IFO 12010.…”

Section: An Attempt To Purify the C-p Bond Cleavage Enzyme In E Aeromentioning

confidence: 71%

“…As to the C-P bond cleavage in phosphonoacetic acid, we first thought that phosphonoacetic acid is reduced to phosphonoacetaldehyde and then the C-P bond is cleaved by an enzyme, "phosphonatase", as was assumed for the C-P bond cleavage in 2-aminoethylphosphonic acid. 14 ) However, the enzyme we found in E. aerogenes IFO 12010 requires no co factors for its catalytic function. Furthermore, "phosphonatase" was shown to be inactive on alkyl-and phenylphosphonic acids.…”

Section: An Attempt To Purify the C-p Bond Cleavage Enzyme In E Aeromentioning

confidence: 74%

Carbon-Phosphorus Hydrolase: Some Properties of the Enzyme in Cell Extracts ofEnterobacter aerogenes

Murata

Higaki

Kimura

1989

Agricultural and Biological Chemistry

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“…A related transaminase can be found in bacteria adapted for the use of AEP as an alternate source of carbon, nitrogen, and phosphorous. Because the physiological reaction is catalyzed in the direction of Pald formation, this enzyme has become known as AEP transaminase (27)(28)(29)(30)(31). It, too, is dependent on pyridoxal phosphate; however, the ammonium group acceptor is not pyruvate but rather L-glutamate (32).…”

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The Phosphonopyruvate Decarboxylase from Bacteroides fragilis

Zhang

Dai

et al. 2003

Journal of Biological Chemistry

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The enzymic cleavage of the carbon-phosphorus bond: Purification and properties of phosphonatase

Cited by 115 publications

References 54 publications

Insights into the Mechanism of Catalysis by the P−C Bond-Cleaving Enzyme Phosphonoacetaldehyde Hydrolase Derived from Gene Sequence Analysis and Mutagenesis

Insights into the Mechanism of Catalysis by the P−C Bond-Cleaving Enzyme Phosphonoacetaldehyde Hydrolase Derived from Gene Sequence Analysis and Mutagenesis

Carbon-Phosphorus Hydrolase: Some Properties of the Enzyme in Cell Extracts ofEnterobacter aerogenes

The Phosphonopyruvate Decarboxylase from Bacteroides fragilis

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