Specificity of Penicillin Amidases

Claridge, C. A.; Luttinger, J. R.; Lein, Joseph

doi:10.3181/00379727-113-28559

Cited by 44 publications

(17 citation statements)

References 7 publications

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“…u~~w > t . 4 Determination of deactivation constant of the whole-cell penicillin amidohydrolase in hydrolytic reaction. The intact whole-cell penicillin amidohydrolase was incubated at 36°C before hydrolytic reaction.…”

Section: Resultsmentioning

confidence: 99%

Biochemical properties of penicillin amidohydrolase from Micrococcus luteus

Nam¹,

Ryu²

1979

Appl Environ Microbiol

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Some biochemical properties of whole-cell penicillin amidohydrolase from Micrococcus luteus have been studied. This whole-cell enzyme showed its maximal activity at 36°C at pH 7.5. It was found that the activation energy of this enzyme was 8.03 kcal (ca. 33.6 kJ) per mol, and this amidohydrolase showed firstorder decay at 360C. The penicillin amidohydrolase was deactivated rapidly at temperatures above 500C during storage or preincubation for 24 h. The Michaelis constant, Ki, for penicillin G was determined as 2.26 mM, and the substrate inhibition constant, K"8, was 155 mM. The whole-cell penicillin amidohydrolase from M. luteus was capable of hydrolyzing penicillin G, penicillin V, ampicillin, and cephalexin, but not cephalosporin C and cloxacillin. This whole-cell enzyme also had synthetic activity for semisynthetic penicillins or cephalosporins from D-(-)-a-phenylglycine methyl ester and 6-a-aminopenicillanic acid or 7-amino-3deacetoxycephalosporanic acid.

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Section: Resultsmentioning

confidence: 99%

Biochemical properties of penicillin amidohydrolase from Micrococcus luteus

Nam¹,

Ryu²

1979

Appl Environ Microbiol

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“…Many of the findings reported in the early Japanese work were confirmed later [8][9][10]. Whilst there were some inconsistencies, in particular the fact that the reported melting point of penicin differed from that of authentic 6-APA, there seems little doubt that both Murao's 'penicin' and Kato's 'penicillin nucleus' were 6-APA.…”

Section: Work In Japan During the 1950smentioning

confidence: 58%

Development of the semi-synthetic penicillins and cephalosporins

Hamilton‐Miller¹

2008

International Journal of Antimicrobial Agents

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“…Therefore, enzymes can be grouped as those that hydrolyse penicillin G, penicillin V, or ampicillin. In 1963 it was suggested to divide penicillin acylases into classes I and II [2]. Class I enzymes basically hydolyse penicillin V (phenoximethylpenicillin), while class II enzymes use penicillin G (benzylpenicillin) as a substrate.…”

Section: Classification Of Penicillin Acylasesmentioning

confidence: 99%