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Information on EC 3.5.1.11 - penicillin amidase and Organism(s) Priestia megaterium and UniProt Accession Q60136

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EC Tree
     3 Hydrolases
         3.5 Acting on carbon-nitrogen bonds, other than peptide bonds
             3.5.1 In linear amides
                3.5.1.11 penicillin amidase
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This record set is specific for:
Priestia megaterium
UNIPROT: Q60136 not found.
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The taxonomic range for the selected organisms is: Priestia megaterium
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
amidohydrolase, penicillin g acylase, penicillin acylase, penicillin amidase, penicillin v acylase, penicillin g amidase, sm-pva, kcpga, afpga, penicillin-g acylase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
penicillin G acylase
-
alpha-acylamino-beta-lactam acylhydrolase
-
-
-
-
ampicillin acylase
-
-
-
-
benzylpenicillin acylase
-
-
-
-
novozym 217
-
-
-
-
penicillin acylase
Penicillin amidohydrolase
penicillin G acylase
Penicillin G amidase
-
-
-
-
Penicillin G amidohydrolase
-
-
-
-
penicillin V acylase
-
-
-
-
Penicillin V amidase
-
-
-
-
semacylase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of peptide bond
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
penicillin amidohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9014-06-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
penicillin + H2O
a carboxylate + 6-aminopenicillanate
show the reaction diagram
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
show the reaction diagram
-
-
-
?
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
show the reaction diagram
-
-
-
?
3-nitro-6-phenylacetaminobenzoic acid + H2O
6-nitrophenol + ?
show the reaction diagram
-
-
-
-
?
3-nitro-6-phenylacetaminobenzoic acid + H2O
?
show the reaction diagram
-
-
-
-
?
6-nitro-3-(phenylacetamido)benzoic acid + H2O
phenylacetic acid + 5-amino-2-nitrobenzoic acid
show the reaction diagram
-
-
-
-
?
7-amino-desacetoxycephalosporanic acid + D-alpha-phenylglycine methylester
?
show the reaction diagram
-
acylating activity
-
-
?
7-amino-desacetoxycephalosporanic acid + D-phenylglycine amide
cephalexin
show the reaction diagram
-
high reactant concentrations
-
-
r
7-aminocephalosporanic acid + D-alpha-phenylglycine methylester
?
show the reaction diagram
-
acylating activity
-
-
?
allylmercaptomethylpenicillin + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
show the reaction diagram
beta-(alpha-toluylamido)-propionic acid + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
cefamandole + H2O
(6R,7R)-7-amino-3-{[(1-methyl-1H-tetrazol-5-yl)sulfanyl]methyl}-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid + (2R)-hydroxy(phenyl)acetic acid
show the reaction diagram
-
-
-
-
?
cephalexin + H2O
(2R)-2-[(R)-[[(2R)-2-amino-2-phenylacetyl]amino](carboxy)methyl]-5-methyl-3,6-dihydro-2H-1,3-thiazine-4-carboxylic acid
show the reaction diagram
-
-
-
-
?
cephaloglycin + H2O
?
show the reaction diagram
-
-
-
-
?
cephaloridine + H2O
(6R,7R)-7-amino-8-oxo-3-[(pyridin-1-ium-1-yl)methyl]-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylate + (thiophen-2-yl)acetic acid
show the reaction diagram
-
-
-
-
?
cephalosporin G + H2O
7-amino-desacetoxycephalosporanic acid + phenylacetic acid
show the reaction diagram
-
-
-
-
?
cephalosporin G + H2O
phenylacetic acid + 7-aminodeacetoxycephalosporanate
show the reaction diagram
-
-
-
-
?
cephalothin + H2O
(6R,7R)-3-[(acetyloxy)methyl]-7-amino-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid + (thiophen-2-yl)acetic acid
show the reaction diagram
-
-
-
-
?
cephradine + H2O
(2R)-amino(cyclohexa-1,4-dien-1-yl)acetic acid + (6R,7R)-7-amino-3-methyl-8-oxo-5-thia-1-azabicyclo[4.2.0]oct-2-ene-2-carboxylic acid
show the reaction diagram
-
-
-
-
?
D,L-N-phenylacetylalanine + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
delta2-pentenylpenicillin + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
ethylthiomethylpenicillin + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
N-methylphenylacetamide + H2O
?
show the reaction diagram
-
poor substrate
-
-
?
penicillin G + H2O
6-aminopenicillanate + phenylacetic acid
show the reaction diagram
-
-
-
?
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
show the reaction diagram
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
show the reaction diagram
penicillin V + H2O
6-aminopenicillanic acid + phenoxyacetic acid
show the reaction diagram
-
poor substrate
-
-
?
penicillin V + H2O
phenoxyacetic acid + 6-aminopenicillanate
show the reaction diagram
-
-
-
-
?
penicillin-G + H2O
6-aminopenicillanic acid + phenylacetic acid
show the reaction diagram
-
-
-
-
?
phenoxyethylpenicillin + H2O
3-phenoxypropanoic acid + 6-aminopenicillanic acid
show the reaction diagram
-
poor substrate
-
-
?
phenylacetamide + H2O
?
show the reaction diagram
phenylacetamide + H2O
NH3 + ?
show the reaction diagram
-
poor substrate
-
-
?
[(2R,3S),(2S,3R)]-cis-3-amino-azetidinone + phenoxy-acetic acid methyl ester
(2R,3S)-beta-lactam intermediate + methanol
show the reaction diagram
-
-
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
penicillin + H2O
a carboxylate + 6-aminopenicillanate
show the reaction diagram
-
-
-
?
benzylpenicillin + H2O
phenylacetic acid + 6-aminopenicillanate
show the reaction diagram
penicillin G + H2O
6-aminopenicillanic acid + phenylacetic acid
show the reaction diagram
penicillin G + H2O
phenylacetic acid + 6-aminopenicillanate
show the reaction diagram
penicillin V + H2O
phenoxyacetic acid + 6-aminopenicillanate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
autoproteolytic processing of the alpha and beta subunit
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6-aminopenicillanate
-
product inhibition
6-aminopenicillanic acid
-
non-competitive inhibition
phenylacetic acid
additional information
-
no inhibition with sulfhydryl reagents
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.83
penicillin G
pH and temperature not specified in the publication
4.5
benzylpenicillin
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
26
6-aminopenicillanate
-
37°C, pH 8.7
450
phenylacetic acid
-
37°C, pH 8.7
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01
-
nitrophenylacetylaminobenzoic acid as substrate, purified F145A mutant enzyme, 37°C
0.04
-
nitrophenylacetylaminobenzoic acid as substrate, purified F145L mutant enzyme, 37°C
0.19
-
ampicillin as subsrate, purified enzyme, 37°C, pH 6.8
0.23
-
cephradine as subsrate, purified enzyme, 37°C, pH 6.8
0.56
-
cephalexin as subsrate, purified enzyme, 37°C, pH 6.8
0.67
-
cephaloglycin as subsrate, purified enzyme, 37°C, pH 6.8
0.85
-
7-amino-desacetoxycephalosporanic acid + D-phenylglycine amide as substrates, purified Y144R mutant enzyme, 30°C, pH 7.0
0.904
-
7-amino-desacetoxycephalosporanic acid + D-phenylglycine amide as substrates, purified Y144R/V24F mutant enzyme, 30°C, pH 7.0
1.22
-
nitrophenylacetylaminobenzoic acid as substrate, purified Y144R/V24F mutant enzyme, 37°C
1.24
-
cephaloridine as subsrate, purified enzyme, 37°C, pH 6.8
1.36
-
cefamandole as subsrate, purified enzyme, 37°C, pH 6.8
1.48
-
7-amino-desacetoxycephalosporanic acid + D-phenylglycine amide as substrates, purified V24F mutant enzyme, 30°C, pH 7.0
1.49
-
7-amino-desacetoxycephalosporanic acid + D-phenylglycine amide as substrates, purified native enzyme, 30°C, pH 7.0
1.58
-
cephalothin as subsrate, purified enzyme, 37°C, pH 6.8
1.86
-
penicillin G as subsrate, purified enzyme, 37°C, pH 6.8
1.94
-
7-amino-desacetoxycephalosporanic acid + D-phenylglycine amide as substrates, purified F145Y mutant enzyme, 30°C, pH 7.0
182
-
immobilized enzyme, pH 8.0, 37°C
22.1
-
nitrophenylacetylaminobenzoic acid as substrate, purified Y144R mutant enzyme, 37°C
3.35
-
nitrophenylacetylaminobenzoic acid as substrate, purified V24F mutant enzyme, 37°C
30.6
-
nitrophenylacetylaminobenzoic acid as substrate, purified native enzyme, 37°C
31.7
-
substrate benzylpenicillin, purified enzyme, 37°C, pH 8.7
9.73
-
nitrophenylacetylaminobenzoic acid as substrate, purified F145Y mutant enzyme, 37°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
overview on values for similar organisms
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5 - 10
-
steep increase in activity up to pH 6.5, approximately 75% of activity at pH 10
7.5 - 9.5
-
rapid decrease in activity when the pH is raised above 9.5 or lowered below 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57
-
unstable at optimum temperature
additional information
-
overview on values for similar organisms
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
-
75% of maximum activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
1000 U/ml, 10 mg/ml
Manually annotated by BRENDA team
-
51 g/l of casein hydrolyzed with Alcalase and 2.7 g/l of phenylacetic acid (PhAc), the following carbon substrates are tested, individually and combined: glucose, glycerol, and lactose (present in cheese whey). Glycerol and glucose are effective nutrients for the microorganism growth but delay the penicillin G acylase production. Cheese whey always increases enzyme production and cell mass. However lactose (present in cheese whey) is not a significant carbon source for Bacillus megaterium. Phenylacetic acid, amino acids, and small peptides present in the hydrolyzed casein are the actual carbon sources for enzyme production. Replacement of hydrolyzed casein by free amino acids, 10.0 g/l, leads to a significant increase in enzyme production (approximately 150%), with a preferential consumption of alanine, aspartic acid, glycine, serine, arginine, threonine, lysine, and glutamic acid. A decrease of the enzyme production is observed when 20.0 g/l of amino acids are used. Using the single omission technique, it is shown that none of the 18 tested amino acids is essential for enzyme production. The use of a medium containing eight of the preferentially consumed amino acids leads to similar enzyme production level obtained when using 18 amino acids. Phenylacetic acid, up to 2.7 g/l, does not inhibit enzyme production, even if added at the beginning of the cultivation
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
The enzyme catalyzes the hydrolysis of the amidic bonds of penicillin G and cephalosporin G to produce key components in the synthesis of beta-lactam antibiotics
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PAC_PRIMG
802
1
91988
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
115000
-
gel filtration
120000
26900
-
1 * 26900 + 1 * 59100, SDS-PAGE
27000
27753
-
1 * 27753 + 1 * 61394, alpha,beta, calculated from the deduced amino acid sequence
57000
59100
-
1 * 26900 + 1 * 59100, SDS-PAGE
61394
-
1 * 27753 + 1 * 61394, alpha,beta, calculated from the deduced amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
alpha and beta chain
dimer
heterodimer
-
1 * 26900 + 1 * 59100, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
proteolytic modification
-
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
F145A
-
alpha chain, no formation of cephalexin, no activity with nitrophenylacetylaminobenzoic acid
F145L
-
alpha chain, no formation of cephalexin, no activity with nitrophenylacetylaminobenzoic acid
F145Y
-
alpha chain, slightly increased formation of cephalexin, 32% of nitrophenylacetylaminobenzoic acid hydrolyzing activity
K427A
K430A
K430A/K427A
-
mutation in beta-chain. Mutant shows a good stability to solvent and thermostability
V24F
-
beta chain, no effect on the formation of cephalexin, 11% of nitrophenylacetylaminobenzoic acid hydrolyzing activity
Y144R
-
alpha chain, reduced formation of cephalexin, 72% of nitrophenylacetylaminobenzoic acid hydrolyzing activity
Y144R/V24F
-
Y144R on alpha chain, V24F on beta chain, reduced formation of cephalexin, 4% of nitrophenylacetylaminobenzoic acid hydrolyzing activity
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 4.8
-
high inactivation at pH 4.0, but stable at pH 4.8
711120
5 - 9
-
almost fully stable upon incubation at 37°C
678562
6.5 - 10
-
highest stability when incubated at 24°C for 9 h
680527
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
-20
-
pH 8.4, protein concentration of 1 mg/ml, stable for at least 8 hours
24
-
pH 8.4, protein concentration of 1 mg/ml, stable for at least 8 hours
37
-
pH 8.4, protein concentration of 1 mg/ml, stable for at least 8 hours
40
-
fully stable at temperatures up to 40°C upon 1 h incubation at 8.5°C
45
-
pH 8.4, protein concentration of 1 mg/ml, 70% of activity lost within 8 hours
5
-
pH 8.4, protein concentration of 1 mg/ml, stable for at least 8 hours
50
-
60% of initial activity lost upon 1 h incubation at 8.5°C
57
-
unstable at the optimum temperature
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
4°C, 0.05 M phosphate buffer, pH 7.0, purified enzyme, stable for at least 3 months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
from cell culture medium of transgenic Bacillus subtilis
-
native and mutant proteins
-
native enzyme 12.7fold from fermentation broth by expanded bed adsorption method using a cationic resin, method comparisons show similar results for packed-bed and for expanded-bed modes, evaluation, overview
-
recombinant enzyme from Bacillus megaterium UN-cat
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli HB101, enzyme is expressed as cytoplasmic enzyme, enzyme production not inducible by phenylacetic acid, expressed in Escherichia coli TG1, enzyme production inducible by addition of IPTG, intracellular expression
expressed in Bacillus megaterium MS941, strain is deficient in the major extracellular protease NprM due to deletion of the corresponding gene, expressed in the newly constructed Bacillus megaterium YYBm1 strain, which has a xylose utilization deficiency, 7fold higher enzyme expression compared with host strain
-
expressed in enzyme deficient Bacillus megaterium strain UN-cat, 20fold higher expression rate than in host strain
-
expressed in Escherichia coli and Bacillus subtilis, high expression rate of extracellular enzyme in Bacillus subtilis
-
expressed in Escherichia coli MC1061
-
native and mutant proteins expresses in Bacillus subtilis WB600
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
production of 6-aminopenicillanate as precursor for the production of semi-synthetic beta-lactam derivatives
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Savidge, T.A.; Cole, M.
Penicillin acylase (bacterial)
Methods Enzymol.
43
705-721
1975
Priestia megaterium, Escherichia coli
Manually annotated by BRENDA team
Zaks, A.; Dodds, D.R.
Application of biocatalysts and biotransformation to the synthesis of pharmaceuticals
Drug Discov. Today
2
513-531
1997
Priestia megaterium
-
Manually annotated by BRENDA team
Pinotti, L.M.; Silva, A.F.; Silva, R.G.; Giordano, R.L.
Study of different media for production of penicillin G acylase from Bacillus megaterium ATCC 14945
Appl. Biochem. Biotechnol.
84-86
655-663
2000
Priestia megaterium
Manually annotated by BRENDA team
Pinotti, L.M.; Silva, R.G.; Giordano, R.C.; Giordano, R.L.
Inoculum studies in production of penicillin G acylase by Bacillus megaterium ATCC 14945
Appl. Biochem. Biotechnol.
98-100
679-686
2002
Priestia megaterium
Manually annotated by BRENDA team
Wang, J.; Zhang, Q.; Huang, H.; Yuan, Z.; Ding, D.; Yang, S.; Jiang, W.
Increasing synthetic performance of penicillin G acylase from Bacillus megaterium by site-directed mutagenesis
Appl. Microbiol. Biotechnol.
74
1023-1030
2007
Priestia megaterium
Manually annotated by BRENDA team
Illanes, A.; Torres, R.; Cartagena, O.; Ruiz, A.
Evaluation of penicillin acylase production by two strains of Bacillus megaterium
Biol. Res.
26
357-364
1993
Priestia megaterium
Manually annotated by BRENDA team
Acevedo, F.; Cooney, C.L.
Pencillin amidase production by Bacillus megaterium
Biotechnol. Bioeng.
15
493-503
1973
Priestia megaterium
Manually annotated by BRENDA team
Zhang, L.F.; Li, Z.W.; Zhang, Q.J.
Cloning and expression of penicillin G acylase gene in Bacillus megaterium
Chin. J. Biotechnol.
7
63-72
1991
Priestia megaterium, Priestia megaterium BM1
Manually annotated by BRENDA team
Martin, L.; Prieto, M.A.; Cortes, E.; Garcia, J.L.
Cloning and sequencing of the pac gene encoding the penicillin G acylase of Bacillus megaterium ATCC 14945
FEMS Microbiol. Lett.
125
287-292
1995
Priestia megaterium (Q60136)
Manually annotated by BRENDA team
Panbangred, W.; Weeradechapon, K.; Udomvaraphant, S.; Fujiyama, K.; Meevootisom, V.
High expression of the penicillin G acylase gene (pac) from Bacillus megaterium UN1 in its own pac minus mutant
J. Appl. Microbiol.
89
152-157
2000
Priestia megaterium
Manually annotated by BRENDA team
Chiang, C.; Bennett, R.E.
Purification and properties of penicillin amidase from Bacillus megaterium
J. Bacteriol.
93
302-308
1967
Priestia megaterium, Priestia megaterium 14945
Manually annotated by BRENDA team
Kang, J.H.; Hwang, Y.; Yoo, O.J.
Expression of penicillin G acylase gene from Bacillus megaterium ATCC 14945 in Escherichia coli and Bacillus subtilis
J. Biotechnol.
17
99-108
1991
Priestia megaterium
Manually annotated by BRENDA team
Yang, Y.; Biedendieck, R.; Wang, W.; Gamer, M.; Malten, M.; Jahn, D.; Deckwer, W.D.
High yield recombinant penicillin G amidase production and export into the growth medium using Bacillus megaterium
Microb. Cell Fact.
5
36
2006
Priestia megaterium
Manually annotated by BRENDA team
Pinotti, L.M.; Ribeiro de Souza, V.; de Campos Giordano, R.; de Lima Camargo Giordano, R.
The penicillin G acylase production by B. megaterium is amino acid consumption dependent
Biotechnol. Bioeng.
97
346-353
2007
Priestia megaterium
Manually annotated by BRENDA team
Chandel, A.K.; Rao, L.V.; Narasu, M.L.; Singh, O.V.
The realm of penicillin G acylase in beta-lactam antibiotics
Enzyme Microb. Technol.
42
199-207
2008
Priestia megaterium, Escherichia coli, Kluyvera cryocrescens
-
Manually annotated by BRENDA team
Massolini, G.; Temporini, C.; Calleri, E.
Penicillin G acylase as chiral selector in LC and CE: exploring the origins of enantioselectivity
J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.
875
20-29
2008
Rhizobium viscosum, Priestia megaterium, Escherichia coli, Kluyvera cryocrescens
Manually annotated by BRENDA team
Pinotti, L.; Fonseca, L.; Prazeres, D.; Rodrigues, D.; Nucci, E.; Giordano, R.
Recovery and partial purification of penicillin G acylase from E. coli homogenate and B. megaterium culture medium using an expanded bed adsorption column
Biochem. Eng. J.
44
111-118
2009
Priestia megaterium, Escherichia coli, Priestia megaterium ATCC 14945, Escherichia coli ATCC 9637
-
Manually annotated by BRENDA team
Xue, J.; Wang, A.; Zhou, C.; Shen, S.
Penicillin acylase immobilization depending on macromolecular crowding and catalysis in aqueous-organic medium
Bioprocess Biosyst. Eng.
32
765-772
2009
Priestia megaterium
Manually annotated by BRENDA team
Avinash, V.; Pundle, A.; Ramasamy, S.; Suresh, C.
Penicillin acylases revisited Importance beyond their industrial utility
Crit. Rev. Biotechnol.
36
303-316
2016
Achromobacter sp., Alcaligenes faecalis, Achromobacter xylosoxidans, Bacillus badius, Bacillus subtilis, Lysinibacillus sphaericus, Fusarium oxysporum, Providencia rettgeri, Escherichia coli (P06875), Kluyvera cryocrescens (P07941), Rhizobium viscosum (P31956), Priestia megaterium (Q60136)
Manually annotated by BRENDA team