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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Subunits
Subunits on EC 3.5.1.11 - penicillin amidase
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dimer
heterodimer
homotetramer
monomer
tetramer
additional information
x * 27000, alpha-subunit, + x * 62400, beta-subunit, SDS-PAGE
?
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alpha,beta, x * 20500 + x * 69000, 23000 Da polypeptide instead of 20500 subunit in vivo, chromatographic and electrophoretic analysis
?
x * 25500, alpha-subunit, + x * 61900, beta-subunit, SDS-PAGE
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1 * 27000 + 1 * 57000, alpha, beta subunits produced by autoproteolytic cleavage, SDS-PAGE
dimer
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1 * 27000 + 1 * 57000, alpha, beta, SDS-PAGE, the alpha and beta subunits range from residue 25 to 265 and from 266 to 802
dimer
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1 * 27753 + 1 * 61394, alpha,beta, calculated from the deduced amino acid sequence
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subunits: 209 amino acids (subunit a) and 557 amino acids (subunit b)
heterodimer
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the enzyme belongs to N-terminal nucleophile hydrolases that share a common fold around the active site bearing a catalytic serine, cysteine, or threonine at the N-terminal position
heterodimer
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the enzyme belongs to N-terminal nucleophile hydrolases that share a common fold around the active site bearing a catalytic serine, cysteine, or threonine at the N-terminal position
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heterodimer
1 * 23000 (alpha-subunit) + 1 * 63000 (beta-subunit)
heterodimer
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1 * 24500, alpha-subunit, + 1 * 65000, beta-subunit, SDS-PAGE, the subunits are held together by noncovalent forces
heterodimer
1 * 18790 (alpha-subunit) + 1 * 60090 (beta-subunit), MALDI-TOF
heterodimer
1 * 21400 (alpha-subunit) + 1 * 59000 (beta-subunit), SDS-PAGE, the beta-subunit loses a fragment of 11000 Da when the enzyme is stored at 4°C , although the enzyme remains active, indicating that the 11000 Da fragment remains attached to the enzyme via noncovalent bonds and that the structure of the enzyme is not affect by the proteolytic effect
heterodimer
Streptomyces lavendulae subsp. lavendulae ATCC 13664
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1 * 18790 (alpha-subunit) + 1 * 60090 (beta-subunit), MALDI-TOF
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heterodimer
Streptomyces lavendulae subsp. lavendulae ATCC 13664
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1 * 21400 (alpha-subunit) + 1 * 59000 (beta-subunit), SDS-PAGE, the beta-subunit loses a fragment of 11000 Da when the enzyme is stored at 4°C , although the enzyme remains active, indicating that the 11000 Da fragment remains attached to the enzyme via noncovalent bonds and that the structure of the enzyme is not affect by the proteolytic effect
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heterodimer
1 * 26000, alpha-subunit, + 1 * 63000, beta-subunit, recombinant His-tagged enzyme, SDS-PAGE
4 * 39191, matrix-associated laser desorption ionization-mass spectrometry
tetramer
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4 * 39191, matrix-associated laser desorption ionization-mass spectrometry
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additional information
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penicillin acylases share a common structural fold and possess a catalytic serine or cysteine or threonine residue at the N-terminal end
additional information
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penicillin G acylase is a 86-kDa heterodimeric protein produced by intein-mediated auto-splicing of a 92-kDa precursor