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Information on EC 3.5.1.93 - glutaryl-7-aminocephalosporanic-acid acylase and Organism(s) Brevundimonas diminuta and UniProt Accession Q9L5D6
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3.5.1.93 glutaryl-7-aminocephalosporanic-acid acylaseIUBMB Comments
Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C.
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Word Map
- 3.5.1.93
- penicillin
-
semisynthetic
- acylases
-
deacylation
-
d-amino
- synthesis
-
autoproteolytic
- beta-lactam
- diminuta
- acremonium
-
7-adca
-
alphabeta2
- industry
- biotechnology
- pharmacology
The taxonomic range for the selected organisms is: Brevundimonas diminuta
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Reaction Schemes
Synonyms
cephalosporin acylase, gl-7-aca acylase, cephalosporin c acylase, glutaryl-7-aminocephalosporanic acid acylase, glutaryl acylase, cpc acylase, scpcacy, gl-7aca acylase, glutaryl-7-aca acylase, j1 acylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GLA
glutaryl-7-ACA acylase
-
glutaryl-7-ACA acylases and cephalosporin acylases have been collectively referred to as cephalosporin acylases because they all have either glutaryl-7-aminocephalosporanic acid or cephalosporin C as their substrates
glutaryl-7-aminocephalosporanic acid acylase
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
(7R)-7-(4-carboxybutanamido)cephalosporanate amidohydrolase
Forms 7-aminocephalosporanic acid, a key intermediate in the synthesis of cephem antibiotics. It reacts only weakly with cephalosporin C.
CAS REGISTRY NUMBER
COMMENTARY
56645-46-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glutaryl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanate + glutarate
-
-
-
?
(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O
(7R)-7-aminocephalosporanate + glutarate
-
-
-
?
adipyl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanate + adipate
-
activity is 19% of the activity with glutaryl-7-aminocephalosporanic acid
-
-
?
cephalosporin C + H2O
7-aminocephalosporanic acid + 2-amino-5-hydroxypentanoate
-
-
-
?
glutaryl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanic acid + glutarate
-
-
-
?
N-acetyl cephalosporin C + H2O
acetate + cephalosporin C
-
activity is 1% of the activity with glutaryl-7-aminocephalosporanic acid
-
-
?
succinyl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanate + succinate
-
activity is 32% of the activity with glutaryl-7-aminocephalosporanic acid
-
-
?
cephalosporin C + H2O
cephalosporanic acid + 2-amino-5-hydroxypentanoate
-
-
-
-
?
cephalosporin C + H2O
cephalosporanic acid + 2-amino-5-hydroxypentanoate
-
activity is 4% of the activity with glutaryl-7-aminocephalosporanic acid
-
-
?
glutaryl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanate + glutarate
-
-
-
-
?
glutaryl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanate + glutarate
-
rate of synthesis is fold slower than rate of synthesis
-
-
r
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O
(7R)-7-aminocephalosporanate + glutarate
-
-
-
?
cephalosporin C + H2O
7-aminocephalosporanic acid + 2-amino-5-hydroxypentanoate
-
-
-
?
glutaryl-7-aminocephalosporanic acid + H2O
7-aminocephalosporanic acid + glutarate
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8
-
activity decrease from pH 7 to pH 9, synthesis of glutaryl-7-aminocephalosporanic acid
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 55
-
30°C: about 45% of maximal activity, 55°C: about 70% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
26000
58000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the enzym is composed of 54 kDa alpha-subunits and 20 kDa beta-subunits
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
the enzyme is translated as an inactive single chain precursor, being post-translationally modified into an active enzyme. The post-translational modification takes place in two steps. The first intramolecular autocatalytic proteolysis takes place at one end of the spacer peptide by a nucleophilic Ser or Thr, which in turn becomes a new N-terminal Ser or Thr. The second intermolecular modification cleaves off the other end of the spacer peptide by another enzyme molecule
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ligand bound enzyme crystals grow at 21°C from hanging drops, binary complex structure of the enzyme with glutaryl-7-aminocephalosporanic acid and glutarate solved at 2.6 A and 2.5 A resolution, respectively, shows extensive interactions between the glutaryl moiety of glutaryl-7-aminocephalosporanic acid and the seven residues that form the side-chain pocket
vapour diffusion method. Binary complex structures with glutarate and glutaryl-7-aminocephalosporanic acid, solved at 2.6 A and 2.5 A resolution, respectively
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F177H
beta-subunit mutant, 17.6% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
F177P
beta-subunit mutant, only partial intramolecular cleavage and no intermolecular cleavage in posttranslational modification, no activity with glutaryl-7-aminocephalosporanic acid
F177T
beta-subunit mutant, 4.3% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate. Only partial intermolecular cleavage in posttranslational modification
Q50L
beta-subunit mutant, 9.9% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
Q50M
beta-subunit mutant, 7.5% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
Q50R
beta-subunit mutant, 2.1% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
Q50T
beta-subunit mutant, 72.5% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
Q50Y
beta-subunit mutant, 15.7% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
R57C
beta-subunit mutant, no intermolecular cleavage in posttranslational modification, no activity with glutaryl-7-aminocephalosporanic acid
R57I
beta-subunit mutant, no intermolecular cleavage in posttranslational modification, no activity with glutaryl-7-aminocephalosporanic acid
R57K
beta-subunit mutant, 0.3% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate, only partial intermolecular cleavage in posttranslational modification
S1A
beta-subunit mutant, no processing takes place, no activity with glutaryl-7-aminocephalosporanic acid
S1C
beta-subunit mutant, no intermolecular cleavage in posttranslational modification, no activity with glutaryl-7-aminocephalosporanic acid
Y149C
alpha-subunit mutant, 16.4% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
Y149G
alpha-subunit mutant, 0.7% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
Y149L
alpha-subunit mutant, 6.3% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
Y149N
alpha-subunit mutant, 30.8% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
Y149P
alpha-subunit mutant, 1.1% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
Y149R
alpha-subunit mutant, 13.6% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
Y33F
beta-subunit mutant, 65.4% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate
Y33I
beta-subunit mutant, 9.3% of the wild-type activity with glutaryl-7-aminocephalosporanic acid as substrate only partial intermolecular cleavage in posttranslational modification
Y33S
beta-subunit mutant, no intermolecular cleavage in posttranslational modification, no activity with glutaryl-7-aminocephalosporanic acid
F177H
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 17.6% of the wild-type activity, no activity with cephalosporin C
F177P
-
beta-subunit mutant, no activity with glutaryl-7-aminocephalosporanic acid and cephalosporin C
F177T
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 4.3% of the wild-type activity, no activity with cephalosporin C
L24F
-
beta-subunit mutant, no activity with glutaryl-7-aminocephalosporanic acid, activity with cephalosporin C is 25.9% of the wild-type activity
L24G
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 27% of the wild-type activity, no activity with cephalosporin C
L24K
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 1.1% of the wild-type activity, no activity with cephalosporin C
L24R
-
beta-subunit mutant, no activity with glutaryl-7-aminocephalosporanic acid, activity with cephalosporin C is 87.7% of the wild-type activity
L24W
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 11.3% of the wild-type activity, activity with cephalosporin C is 98.8% of wild-type activity
Q50L
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 9.9% of the wild-type activity, no activity with cephalosporin C
Q50M
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 7.5% of the wild-type activity, activity with cephalosporin C is 180% of wild-type activity
Q50M/F58A
-
beta-subunit mutation, activity with cephalosporin C is 180% of wild-type activity
Q50M/F58D
-
beta-subunit mutation, activity with cephalosporin C is 130% of wild-type activity
Q50M/F58G
-
beta-subunit mutation, activity with cephalosporin C is 290% of wild-type activity
Q50M/F58H
-
beta-subunit mutation, activity with cephalosporin C is 160% of wild-type activity
Q50M/F58I
-
beta-subunit mutation, activity with cephalosporin C is 150% of wild-type activity
Q50M/F58L
-
beta-subunit mutation, activity with cephalosporin C is 120% of wild-type activity
Q50M/F58P
-
beta-subunit mutation, activity with cephalosporin C is 240% of wild-type activity
Q50M/F58S
-
beta-subunit mutation, activity with cephalosporin C is 260% of wild-type activity
Q50M/F58T
-
beta-subunit mutation, activity with cephalosporin C is 230% of wild-type activity
Q50M/Y149F
-
Q50M mutation in beta-subunit, Y149F mutation in alpha-subunit, activity with cephalosporin C is 157% of wild-type activity
Q50M/Y149K
-
Q50M mutation in beta-subunit, Y149K mutation in alpha-subunit, activity with cephalosporin C is 600% of wild-type activity
Q50M/Y149K/F177G
-
beta-subunit mutation, activity with cephalosporin C is 787% of wild-type activity
Q50M/Y149K/F177P
-
beta-subunit mutation, activity with cephalosporin C is 301% of wild-type activity
Q50M/Y149K/F177S
-
beta-subunit mutation, activity with cephalosporin C is 456% of wild-type activity
Q50M/Y149K/M145A
-
Q50M and Y149K are mutation in the beta-subunit, M145A is a mutation in the alpha-subunit, activity with cephalosporin C is 335% of wild-type activity
Q50M/Y149K/M145L
-
Q50M and Y149K are mutations in the beta-subunit, M145L is a mutation in the alpha-subunit, activity with cephalosporin C is 704% of wild-type activity
Q50M/Y149K/M145P
-
Q50M and Y149K are mutations in the beta-subunit, M145P is a mutation in the alpha-subunit, activity with cephalosporin C is 442% of wild-type activity
Q50M/Y149K/M145T
-
Q50M and Y149K are mutation in the beta-subunit, M145T is a mutation in the alpha-subunit, activity with cephalosporin C is 433% of wild-type activity
Q50M/Y149K/Y33N
-
beta-subunit mutation, activity with cephalosporin C is 460% of wild-type activity
Q50M/Y149K/Y33S
-
beta-subunit mutation, activity with cephalosporin C is 568% of wild-type activity
Q50M/Y149K/Y33T
-
beta-subunit mutation, activity with cephalosporin C is 424% of wild-type activity
Q50M/Y33D
-
beta-subunit mutant, activity with cephalosporin C is 450% of wild-type activity
Q50M/Y33G
-
beta-subunit mutant, activity with cephalosporin C is 70% of wild-type activity
Q50M/Y33H
-
beta-subunit mutant, activity with cephalosporin C is 101% of wild-type activity
Q50M/Y33L
-
beta-subunit mutant, activity with cephalosporin C is 202% of wild-type activity
Q50M/Y33N
-
beta-subunit mutant, activity with cephalosporin C is 350% of wild-type activity
Q50M/Y33P
-
beta-subunit mutant, activity with cephalosporin C is 99% of wild-type activity
Q50M/Y33S
-
beta-subunit mutant, activity with cephalosporin C is 60% of wild-type activity
Q50M/Y33T
-
beta-subunit mutant, activity with cephalosporin C is 109% of wild-type activity
Q50M/Y33V
-
beta-subunit mutant, activity with cephalosporin C is 135% of wild-type activity
Q50R
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 2.1% of the wild-type activity, no activity with cephalosporin C
Q50T
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 72.5% of the wild-type activity, no activity with cephalosporin C
Q50Y
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 15.7% of the wild-type activity, no activity with cephalosporin C
R155G
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 88% of the wild-type activity
R57C
-
beta-subunit mutant, no activity with glutaryl-7-aminocephalosporanic acid and cephalosporin C
R57I
-
beta-subunit mutant, no activity with glutaryl-7-aminocephalosporanic acid and cephalosporin C
R57K
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 0.3% of the wild-type activity, no activity with cephalosporin C
R57S
-
beta-subunit mutant, no activity with glutaryl-7-aminocephalosporanic acid and cephalosporin C
S152G
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 75.4% of the wild-type activity, activity with cephalosporin C is 38.6% of wild-type activity
S152H
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 63.7% of the wild-type activity, activity with cephalosporin C is 11.9% of wild-type activity
S152N
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 78% of the wild-type activity, activity with cephalosporin C is 24.8% of wild-type activity
S152P
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 76.2% of the wild-type activity, activity with cephalosporin C is 60.4% of wild-type activity
S152T
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 81.4% of the wild-type activity, activity with cephalosporin C is 34.7% of wild-type activity
S1A
-
beta-subunit mutant, no activity with glutaryl-7-aminocephalosporanic acid and cephalosporin C
S1betaC
-
no activity with glutaryl-7-aminocephalosporanic acid and cephalosporin C
V70G
-
beta-subunit mutant, no activity with glutaryl-7-aminocephalosporanic acid, activity with cephalosporin C is 32.1% of the wild-type activity
V70S
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 28.8% of the wild-type activity, no activity with cephalosporin C
Y149C
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 16.4% of the wild-type activity, activity with cephalosporin C is 24% of wild-type activity
Y149G
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 0.7% of the wild-type activity, no activity with cephalosporin C
Y149L
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 6.3% of the wild-type activity, activity with cephalosporin C is 48% of wild-type activity
Y149N
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 30.8% of the wild-type activity, activity with cephalosporin C is 48% of wild-type activity
Y149P
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 1.1% of the wild-type activity, no activity with cephalosporin C
Y149R
-
alpha-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 13.6% of the wild-type activity, no activity with cephalosporin C
Y33F
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 65.4% of the wild-type activity, no activity with cephalosporin C
Y33I
-
beta-subunit mutant, activity with glutaryl-7-aminocephalosporanic acid is 9.3% of the wild-type activity, activity with cephalosporin C is 90% of wild-type activity
Y33S
-
beta-subunit mutant, no activity with glutaryl-7-aminocephalosporanic acid, activity with cephalosporin C is 120% of the wild-type activity
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
-
1 h, stable at pH 9.0, about 45% less of activity at pH 6, about 15% loss of activity at pH 7, about 10% loss of activity at pH 8, about 60% loss of activity at pH 10
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a modified chitin-binding domain-GLA fusion protein is affinity purified on chitin column by changing the salt concentration of binding and elution buffer
-
ammonium sulfate precipitation, chitin granula column chromatography, and Co2+-iminodiacetic acid-Sepharose column chromatography
-
ammonium sulfate precipitation, Toyopearl HW65F column chromatography, and CM Toyopearl 650 column chromatography
-
several chemical treatment techniques commonly used for protein extraction are investigated for recovering glutaryl-7-aminocephalosporanic acid acylase (GLA) from recombinant Escherichia coli cells, best results are obtained by the combined use of 0.5% w/v cetyltrimethylammonium bromide (CTAB) and 0.3 M KCl at 10°C for 12 h, method evaluation and optimization of all extraction parameters, detailed overview
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, recombinant overexpression of the soluble enzyme in Escherichia coli strain BL21(DE3) using vector pET-28a, optimization of culture consitions in the upscaling to 2.0% w/v lactose inducing in YT medium at 25°C, resulting in over 50fold increased enzyme activity and 14470 U/l and 206 U/l/h, overview
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Oh, B.; Kim, M.; Yoon, J.; Chung, K.; Shin, Y.; Lee, D.; Kim, Y.
Deacylation activity of cephalosporin acylase to cephalosporin C is improved by changing the side-chain conformations of active-site residues
Biochem. Biophys. Res. Commun.
310
19-27
2003
Brevundimonas diminuta
Kim, Y.; Hol, W.G.
Structure of cephalosporin acylase in complex with glutaryl-7-aminocephalosporanic acid and glutarate: insight into the basis of its substrate specificity
Chem. Biol.
8
1253-1264
2001
Brevundimonas diminuta (Q9L5D6), Brevundimonas diminuta KAC-1 (Q9L5D6)
Kim, S.; Kim, Y.
Active site residues of cephalosporin acylase are critical not only for enzymatic catalysis but also for post-translational modification
J. Biol. Chem.
276
48376-48381
2001
Brevundimonas diminuta (Q9L5D6)
Aramori, I.; Fukagawa, M.; Tsumura, M.; Iwami, M.; Ono, H.; Ishitani, Y.; Koji, H.; Kohsaka, M.; Ueda, Y.; Imanaka, H.
Comparative characterization of new glutaryl 7-ACA and cephalosporin C acylases
J. Ferment. Bioeng.
73
185-192
1992
Brevibacillus laterosporus, Brevundimonas diminuta, Pseudomonas sp., Brevundimonas diminuta N176, Brevibacillus laterosporus J1
-
Kim, Y.; Yoon, K.; Khang, Y.; Turley, S.; Hol, W.G.
The 2.0 A crystal structure of cephalosporin acylase
Structure Fold. Des.
8
1059-1068
2000
Brevundimonas diminuta (Q9L5D6), Brevundimonas diminuta
Khatuntseva, S.A.; Eldarov, M.A.; Lopatin, S.A.; Zeinalov, O.A.; Skryabin, K.G.
Cloning and expression of variants of the glutaryl-7-aminocephalosporic acid acylase of the bacterium Brevundimonas diminuta in Escherichia coli cells
Appl. Biochem. Microbiol.
43
414-421
2007
Brevundimonas diminuta, Brevundimonas diminuta VKM B-1297
-
Sonawane, V.C.
Enzymatic modifications of cephalosporins by cephalosporin acylase and other enzymes
Crit. Rev. Biotechnol.
26
95-120
2006
Aeromonas sp., Achromobacter xylosoxidans, Arthrobacter sp., Rhizobium viscosum, Brevibacillus laterosporus, Bacillus sp. (in: Bacteria), Brevundimonas diminuta, Burkholderia cepacia, Sphingomonas paucimobilis, Flavobacterium sp., Paecilomyces sp. (in: Eurotiomycetes), Pseudomonas sp., Pseudomonas putida, Pseudomonas nitroreducens, Aeromonas sp. ACY 95, Burkholderia cepacia BY21, Arthrobacter sp. 5-8A, Flavobacterium sp. 650, Pseudomonas sp. A14, Brevibacillus laterosporus J1, Pseudomonas nitroreducens CCRC 11041, Bacillus sp. (in: Bacteria) SV12, Pseudomonas sp. BLO 72, Brevundimonas diminuta N 176
Khatuntseva, S.A.; Eldarov, M.A.; Redo, V.A.; Skryabin, K.G.
Purification and immobilization of recombinant variants of Brevundimonas diminuta glutaryl-7-aminocephalosporanic acid acylase expressed in Escherichia coli cells
J. Biotechnol.
133
123-126
2008
Brevundimonas diminuta
Ma, X.; Su, E.; Zhu, Y.; Deng, S.; Wei, D.
High-level expression of glutaryl-7-aminocephalosporanic acid acylase from Pseudomonas diminuta NK703 in Escherichia coli by combined optimization strategies
J. Biotechnol.
168
607-615
2013
Brevundimonas diminuta (G3MDB2), Brevundimonas diminuta, Brevundimonas diminuta NK703 (G3MDB2)
Ma, X.; Su, E.; Deng, S.; Wei, D.
An effective method for extraction of glutaryl-7-aminocephalosporanic acid acylase from recombinant E. coli cells
Biotechnol. Bioprocess Eng.
20
718-724
2015
Brevundimonas diminuta (G3MDB2), Brevundimonas diminuta NK703 (G3MDB2)
-
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