Purification and properties of methioninase from <i>Pseudomonas ovalis</i>

Tanaka, Hidehiko; Esaki, Nobuyoshi; Yamamoto, Tatsuo; Soda, Kenji

doi:10.1016/0014-5793(76)80528-5

Cited by 64 publications

(51 citation statements)

References 12 publications

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“…In addition, our data in agreement with (El-sayed, 2011) who mentioned that the isoelectric point of the enzyme was pH 4.8 and the lower enzyme stability in acidic conditions may be due to the closeness of his enzyme to the isoelectric point. The pH stability of the enzyme from other sources was over range from 7 to 8 (Dias and Weimmer, 1998;Tanaka et al,. 1976).…”

Section: Effect Of Ph On the Enzyme Activity And Stabilitymentioning

confidence: 99%

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Purification and characterization of a novel thermo stable L-methioninase from Streptomyces sp. DMMMH4 and its evaluation for anticancer activity

Selim¹,

Saad²,

Mostafa³

et al. 2016

J App Pharm Sci

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L-methioninase has been purified 2.55-fold from the crude extract of Streptomyces sp. DMMMH4. The purification procedure was carried out by heat treatment and gel filtration on Sephadex G-200 column chromatography. SDS-PAGE electrophoresis showed a migrating protein band molecular mass of 47 kDa. The kinetic properties determined for the purified enzyme displayed optimum activity at 70 O C and thermal stability were 70 O C for 30 min. The enzyme showed maximum activity at pH 6 using acetate buffer 0.05M and was relatively stable across a broad range of pH values (5.5-8 pH). The enzyme strongly inhibited by Cr +2 , Fe +2 , Ni +2 , Cd +2 , PMSF, β-mercaptoethanol and SDS while Hg +2 ,Cu +2 and iodoacetate completely inhibited the enzyme activity at a final concentration of 10mM. The purified enzyme exhibited a Km of 0.7, 0.15 and 0.25 mM for L-methionine, DL-ethionine and L-cystine respectively. Cytotoxicity test demonstrate that enzyme was active against liver HepG2, breast MCF-7, lung A549, prostate PC3 and colon HCT116 cancer cell lines and has negligible toxicity toward a normal melanocyte cell line HFB4.

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Section: Effect Of Ph On the Enzyme Activity And Stabilitymentioning

confidence: 99%

“…L-methioninase was extensively characterized from various bacterial species especially Pseudomonas. Purification of L-methioninase from Pseudomonas ovalis was carried out by (Tanaka et al, 1976). They reported that, the purified enzyme had a molecular weight of 43KDa.…”

Section: Introductionmentioning

confidence: 99%

Purification and characterization of a novel thermo stable L-methioninase from Streptomyces sp. DMMMH4 and its evaluation for anticancer activity

Selim¹,

Saad²,

Mostafa³

et al. 2016

J App Pharm Sci

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“…ovalis), and showed that the enzyme catalyzes a,3,-elimination and 7-replacement reactions of L-methionine and its derivatives, and also a,/3-elimination and 13-replacement reactions of S-substituted-L-cysteines [ 1,2]. A Schiff base between pyridoxamine 5'-phosphate and 2-keto-3-butenoic acid is regarded as a key intermediate in the a,7-elimination (1) and 7-replacement (2) reactions as reviewed by Snell and Di Mari [3], and Davis and Metzler [4].…”

Section: Introductionmentioning

confidence: 99%

“…[8] and S-substituted homocysteines [2] were prepared as described previously. a-Ketobutyric acid and crystalline lactate dehydrogenase of beef heart were obtained from Sigma, and crystalline (1) (2)…”

Section: Introductionmentioning

confidence: 99%

Deamination and γ‐addition reactions of vinylglycine by L‐methionine γ‐lyase

et al. 1977

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“…Step the Sephadex G-200 gel filtration method [12], with bovine liver catalase (240 000), bacterial methioninase (180 000) [ 13 ], bovine heart lactate dehydrogenase (140 000), bovine serum albumin (monomer, 68 000) and ovalbumin (43 000) as standard proteins. The enzyme shows an absorption spectrum of a simple protein with an A420 1% max.…”

Section: Properties Of the Enzymementioning

confidence: 99%