Microbial Penicillin Acylases

Vandamme, Erick; Voets, J. P.

doi:10.1016/s0065-2164(08)70563-x

Cited by 113 publications

(48 citation statements)

References 242 publications

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“…The penicillin G acylase (penicillin amidase [penicillin amidohydrolase]) EC 3.5.1.11 produced by Escherichia coli W (ATCC 9637) and Proteus rettgeri (ATCC 31052) catalyzes the deacylation of penicillin G. These enzymes are used for commercial production of 6-aminopenicillanic acid, an important precursor for synthesis of many semisynthetic penicillins (17,18).…”

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confidence: 99%

Expression and regulation of the penicillin G acylase gene from Proteus rettgeri cloned in Escherichia coli

Daumy¹,

Williams²,

McColl³

et al. 1986

J Bacteriol

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The penicillin G acylase genes from the Proteus rettgeri wild type and from a hyperproducing mutant which is resistant to succinate repression were cloned in Escherichia coli K-12. Expression of both wild-type and mutant P. rettgeri acylase genes in E. coli K-12 was independent of orientation in the cloning vehicle and apparently resulted from recognition in E. coli of the P. rettgeri promoter sequences. The P. rettgeri acylase was secreted into the E. coli periplasmic space and was composed of subunits electrophoretically identical to those made in P. rettgeri. Expression of these genes in E. coli K-12 was not repressed by succinate as it is in P. rettgeri. Instead, expression of the enzymes was regulated by glucose catabolite repression.

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mentioning

confidence: 99%

Expression and regulation of the penicillin G acylase gene from Proteus rettgeri cloned in Escherichia coli

Daumy¹,

Williams²,

McColl³

et al. 1986

J Bacteriol

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“…This enzyme is very interesting in that it catalyses the transformation of benzylpenicillin into 6-aminopenicillanic acid (dAPA), the precursor of most of the semisynthetic penicillins [8].…”

Section: Methodsmentioning

confidence: 99%

Stabilisation and immobilisation of penicillin amidase

1989

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Pemcdlm amldase was coupled to a penodate-oxrdtsed dextran by reducttve alkylatron m the presence of sodmm cyanoborohydnde A loss of acttvtty (25%) was observed but the conIugate enzyme dextran was more thermostable than the native enzyme Native and dextran-conjugated pemctlhn am&se were rmmobthsed on ammo acttvated sthca (Promaxon, Spherostl, Aerostl) by a classical method usmg ~ut~aldehyde for the nattve enzyme and reducttve alkylatton for the mod&cd enzyme Good relanve acttvrty of the enzymes was obtained after ln~lubill~tion Immobthsatton of both native and mod&d enzymes resulted m the the~ostablhsatlon of the pemcdhn amtdase Enzyme stabrhsatton, Enzyme tmmobthsatton, Pemcdhn amrdase, (Escherrchm co/i)

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“…The enzyme penicillin acylase produced by Escherichia coli, other bacteria and fungi [1], is the basis of this conversion which involves selective hydrolysis of the amide bond in the penicillin side-chain.…”

Section: Introductionmentioning

confidence: 99%

Biotransformations of rifamycins: Process possibilities

Banerjee

Saxena

Chisti

1992

Biotechnology Advances

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Rifampicin, an important antibiotic, is manufactured by chemical conversion of rifamycin S which is obtained by the chemical modification of rifamycin B. Rifamycin B is a product of Nocardia mediterranei fermentations. The chemical conversion of rifamycin B to rifamycin S has many disadvantages: Strong acidic conditions are required, heavy foam formation accompanies transformation and the yields are low. This review highlights the developments in alternative, biochemical transformations using enzymes and cells; the main focus is on transformations carried out by rifamycin oxidase.

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Microbial Penicillin Acylases

Cited by 113 publications

References 242 publications

Expression and regulation of the penicillin G acylase gene from Proteus rettgeri cloned in Escherichia coli

Expression and regulation of the penicillin G acylase gene from Proteus rettgeri cloned in Escherichia coli

Stabilisation and immobilisation of penicillin amidase

Biotransformations of rifamycins: Process possibilities

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