3.5.1.11: penicillin amidase
This is an abbreviated version!
For detailed information about penicillin amidase, go to the full flat file.
Word Map on EC 3.5.1.11
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3.5.1.11
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6-aminopenicillanic
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phenylacetic
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biocatalyst
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anandamide
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acylases
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cannabinoids
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cephalosporin
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synthesis
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binuclear
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alcaligenes
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cephalexin
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megaterium
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endocannabinoids
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semi-synthetic
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3.5.1.1
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kluyvera
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l-asparagine
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dihydroorotase
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phenylacetylated
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allantoinase
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dihydropyrimidinase
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lactonase
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amoxicillin
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rettgeri
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eupergit
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multipoint
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acyl-enzyme
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asparaginase
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hydantoinase
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phenoxyacetic
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aminoacylase
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7-aminocephalosporanic
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phosphotriesterase
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sphaericus
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hydantoin
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providencia
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n-acylethanolamines
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penicillanic
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dihydrouracil
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cleas
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pharmacology
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industry
- 3.5.1.11
-
6-aminopenicillanic
-
phenylacetic
-
biocatalyst
- anandamide
- acylases
- cannabinoids
- cephalosporin
- synthesis
-
binuclear
- alcaligenes
- cephalexin
- megaterium
-
endocannabinoids
-
semi-synthetic
-
3.5.1.1
-
kluyvera
- l-asparagine
- dihydroorotase
-
phenylacetylated
- allantoinase
- dihydropyrimidinase
- lactonase
- amoxicillin
- rettgeri
-
eupergit
-
multipoint
- acyl-enzyme
- asparaginase
- hydantoinase
-
phenoxyacetic
-
aminoacylase
-
7-aminocephalosporanic
- phosphotriesterase
- sphaericus
- hydantoin
- providencia
- n-acylethanolamines
-
penicillanic
- dihydrouracil
-
cleas
- pharmacology
- industry
Reaction
Synonyms
ACPGA001 PGA, AfPGA, alpha-acylamino-beta-lactam acylhydrolase, amidase, amidohydrolase, ampicillin acylase, AuAAC, benzylpenicillin acylase, BmPGA, Eca3205, KcPGA, maPGA, More, novozym 217, PA, PAC, penicillin acylase, penicillin amidase, Penicillin amidohydrolase, penicillin G acylase, Penicillin G amidase, Penicillin G amidohydrolase, penicillin V acylase, Penicillin V amidase, penicillin-G acylase, PGA, PGA650, PVA, semacylase, Sm-PVA, YxeI
ECTree
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Posttranslational Modification
Posttranslational Modification on EC 3.5.1.11 - penicillin amidase
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glycoprotein
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both subunits alpha and beta of the enzyme are N-glycosylated, while the beta-subunit also contains O-glycans , determination of the glycosylation pattern of recombinant enzyme expressed in Pichia pastoris, overview
proteolytic modification
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the enzyme is maturated in vivo from an inactive precursor into the catalytically active enzyme, via a complex post-translational autocatalytic processing with a multi-step excision of a small internal pro-peptide
proteolytic modification
autocatalytical activation via translocation of the precursor to the periplasmic membrane and processing of the precursor by an autocatalytic intramolecular peptide-bond cleavage. Rate-limiting step in the production of active enzyme is the intramolecular autoproteolytic processing of the precursor molecule, resulting in the removal of a linker peptide
proteolytic modification
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intracellular proteolysis in the cytoplasm is one of the important steps that limit the yield of active penicillin amidase from the translational product pre-pro-peniciliin amidase. Glucose and temperature are important parameters, determining the degradation rate of the proteolytically sensitive pre-pro-penicillin amidase
proteolytic modification
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intramolecular autoproteolysis initiates the maturation of penicillin amidase from Escherichia coli. The Gly263-Ser264 bond is hydrolysed first in the free and immobilized mutant proenzyme T263G, this bond is hydrolyzed by intramolecular autoproteolysis
proteolytic modification
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maturation to the of the pro-enzyme occurs during transport through the cytoplasmic membrane or rapidly after its entrance in the periplasm. The pre-pro-enzyme has a MW of 97000 Da, the pro-enzyme a MW of 92000 Da and the B-chain of the penicillin amidase has a MW of 63000 Da
proteolytic modification
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the enzyme is a periplasmic protein, cytoplasmically expressed as a precursor polypeptide comprising a signal sequence, the A and B chains of the mature enzyme, 209 and 557 residues respectively, joined by a spacer peptide of 54 amino acid residues. The wild-type AB heterodimer is produced by proteolytic removal of this spacer in the periplasm. The first step in processing is believed to be autocatalytic hydrolysis of the peptide bond between the C-terminal residue of the spacer and the active-site serine residue at the N-terminus of the B chain. The crystal structure of a slowly processing mutant enzyme reveals that the spacer peptide blocks the entrance to the active site cleft consistent with an autocatalytic mechanism of maturation. For the slowly processed T263G mutant the crystal structure demonstrates a primary cleavage site between Tyr260 and Pro261. This must be followed by a cleavage between Gly263 and Ser264
proteolytic modification
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posttranslational processing steps may occur both in the periplasmand in the cytoplasm
proteolytic modification
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penicillin G acylase is a 86-kDa heterodimeric protein produced by intein-mediated auto-splicing of a 92-kDa precursor
proteolytic modification
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processing of a single enzyme polypeptide precursor, which consists of a small alpha-subunit and a large beta-subunit, to form the heterodimer
proteolytic modification
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the signal peptide is removed from the ppPGA during translocation into the periplasm. In the periplasm pPGA undergoes posttranslational modification that results in active PGA. Processing of the PGA is temperature-dependent
proteolytic modification
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processing of a single enzyme polypeptide precursor, which consists of a small alpha-subunit and a large beta-subunit, to form the heterodimer
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proteolytic modification
the enzyme is synthesized as a single-chain inactive pro-enzyme, which upon autocatalytic processing becomes an active heterodimer of alpha and beta chains. Cleavage of the Thr289-Ser290 bond leads to the unveiling of the primary amine group of Serbeta1 (Ser290 of the precursor), creating the active centre in mature enzyme
proteolytic modification
the enzyme is expressed as a 93000 Da inactive precursor in the cytoplasm which is directed to the periplasmic space by the 26 amino acid residue signal peptide. Subsequently, the spacer peptide is cleaved off by autocatalytic processing to generate the mature and active enzyme
proteolytic modification
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the enzyme is synthesized as a single-chain inactive pro-enzyme, which upon autocatalytic processing becomes an active heterodimer of alpha and beta chains. Cleavage of the Thr289-Ser290 bond leads to the unveiling of the primary amine group of Serbeta1 (Ser290 of the precursor), creating the active centre in mature enzyme
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proteolytic modification
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autoproteolytic cleavage which results in the formation of two subunits, the alpha and beta subunits range from residue 25 to 265 and from 266 to 802 with calculated molecular masses of 27753 Da and 61394 Da, respectively
proteolytic modification
the gene encodes an inactive precursor protein containing a secretion signal peptide that is activated by two internal autoproteolytic cleavages that release a 25-amino-acid linker peptide and two large domains of 18.79 kDa (alpha-subunit) and 60.09 kDa (beta-subunit)
proteolytic modification
Streptomyces lavendulae subsp. lavendulae ATCC 13664
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the gene encodes an inactive precursor protein containing a secretion signal peptide that is activated by two internal autoproteolytic cleavages that release a 25-amino-acid linker peptide and two large domains of 18.79 kDa (alpha-subunit) and 60.09 kDa (beta-subunit)
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