Bacillus subtilis Neutral Proteinase

McConn, James; Tsuru, Daisuke; Yasunobu, Kerry T.

doi:10.1016/s0021-9258(18)91194-4

Cited by 147 publications

(9 citation statements)

References 28 publications

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“…solution for stability. The Bacillus subtilis neutral protease (McConn et al, 1964;Tsuru et al, 1966a,b) as well as the alkaline protease (Tsuru et al, 1966a,b;Matsubara etal., 1958) is stabilized by calcium. Similarly, calcium and other divalent cations stabilize the neutral proteases from Bacillus megaterium (Millet, 1969), Streptomyces griseus (Nomoto et al, 1960), Pseudomonas aeruginosa (Morihara, 1963), and Bacillus cereus (J. , unpublished data).…”

mentioning

confidence: 99%

Role of calcium in thermolysin

Feder¹,

Garrett²,

Wildi³

1971

Biochemistry

145

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confidence: 99%

Role of calcium in thermolysin

Feder¹,

Garrett²,

Wildi³

1971

Biochemistry

145

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“…These results suggest that the enzyme is also a metalloenzyme as is the neutral protease I. [2][3][4] The present paper characterizes B. subtilis neutral protease II to be a zinc metalloenzyme. The enzyme contains 0.19% of zinc which is essential for the enzyme activity and 0.43% of calcium which confers to the enzyme molecule The metals found in stoichiometric ally significant amounts were zinc, 0.19%, and calcium, 0.43%.…”

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confidence: 69%

Studies on Bacterial Protease

TSURU

Kira

Yamamoto

et al. 1966

Agricultural and Biological Chemistry

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The neutral protease of Bacillus amylosacchariticus was inactivated by low concentra tions of several metal-chelating agents and the inactivated enzyme with EDTA restored its activity almost completely by the addition of Zn++ or Co++ and partially by Fell or Mn++, if these metal ions were added shortly after the EDTA-treatment. The native enzyme was found to contain 0.19% of zinc together with a significant amount of calcium. Parallel increase in specific activity and zinc content of enzyme preparation was observed throughout the purification procedure. The elution pattern of enzyme activity on a CM-cellulose column chromatography also completely coincided with that of protein-bound zinc. A zinc-free inactive enzyme was also reactivated by the addition of zinc or cobalt ions, clearly showing that the neutral protease of B. amylosacchariticus is a zinc metalloenzyme.

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“…The bacterial neutral proteases are zinc metalloenzymes (McConn et al, 1964;Tsuru et al, 1966;Hiramatsu, 1967;Matheson and Armstrong;Keay, 1969;Griffin and Prescott, 1970;Keay et al, 1971;Naicajima et al, 1974). Thermolysin, B. subtilis neutral protease, and the neutral protease of Aeromonas proteolytica all actively hydrolyze esters, a feature hitherto unrecognized.…”

Section: Discussionmentioning

confidence: 99%

“…Synthetic peptide substrates have served to detail the specificity of thermolysin and other neutral endopeptidases (see Morihara, 1974 for a review), particularly the marked preference of this class of enzymes for substrates which have hydrophobic amino acids contributing the amino group of the bond to be cleaved. A series of studies has failed to detect esterase activity of neutral proteases when a number of esters, e.g., hippuryl phenyllactate, benzoylarginine ethyl ester, tosylarginine methyl ester, acetyltyrosine ethyl ester, carbobenzoxyglycine p-nitrophenyl ester, and a series of aliphatic alkyl esters served as potential substrates (McConn et al, 1964;Morihara and Tsuzuki, 1966;Feder, 1968). We have now succeeded in synthesizing a series of depsipeptides which are excellent substrates for thermolysin and other neutral proteases.…”

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confidence: 99%

Esterase activity of zinc neutral proteases

Holmquist¹,

Vallée²

1976

Biochemistry

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The hydrolysis of a series of depsipeptides demonstrates that the zinc neutral endopeptidases of bacteria are active esterases. Esters such as BzGly-OPhe-Ala, BzGly-OLeu-Ala, and FA-Gly-OLeu-NH2 are hydrolyzed at rates three- to eightfold slower than are their exact peptide analogues, when hydrolyzed by thermolysin, Bacillus subtilis neutral protease and the neutral protease from Aeromonas proteolytica. Ester hydrolysis by zinc neutral proteases follows the characteristic preference for hydrophobic amino acids adjacent to the site of cleavage, discerned from the hydrolysis of peptide substrates. Removal of zinc from thermolysin abolishes the esterase activity of the native enzyme. Among the metals examined, only Co2+ and Zn2+ restore esterase activity to any significant extent, Co2+ restoring 50% and Zn2+ 100% of the native thermolysin activity. The hydrolysis of esters and peptides by thermolysin does not differ with respect to either the binding or catalytic steps. Substrate specificity, pH-rate profiles, inhibitor, and deuterium isotope effects are identical for both types of substrates.

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Bacillus subtilis Neutral Proteinase

Cited by 147 publications

References 28 publications

Role of calcium in thermolysin

Role of calcium in thermolysin

Studies on Bacterial Protease

Esterase activity of zinc neutral proteases

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