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Information on EC 1.14.11.21 - clavaminate synthase and Organism(s) Streptomyces clavuligerus and UniProt Accession Q05581

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IUBMB Comments
Contains nonheme iron. Catalyses three separate oxidative reactions in the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus. The first step (hydroxylation) is separated from the latter two (oxidative cyclization and desaturation) by the action of EC 3.5.3.22, proclavaminate amidinohydrolase. The three reactions are all catalysed at the same nonheme iron site.
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Streptomyces clavuligerus
UNIPROT: Q05581
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The taxonomic range for the selected organisms is: Streptomyces clavuligerus
The enzyme appears in selected viruses and cellular organisms
Synonyms
clavaminate synthase, clavaminate synthase 2, clavaminic acid synthase, clavaminate synthase 1, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
clavaminate synthase 2
-
clavaminate synthase 1
-
clavaminate synthase 2
-
-
-
-
clavaminic acid synthase
-
-
-
-
synthase, clavaminate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
deoxyamidinoproclavaminate + 2-oxoglutarate + O2 = amidinoproclavaminate + succinate + CO2
show the reaction diagram
proclavaminate + 2-oxoglutarate + O2 = dihydroclavaminate + succinate + CO2 + H2O
show the reaction diagram
dihydroclavaminate + 2-oxoglutarate + O2 = clavaminate + succinate + CO2 + H2O
show the reaction diagram
deoxyamidinoproclavaminate + 2-oxoglutarate + O2 = amidinoproclavaminate + succinate + CO2
show the reaction diagram
proclavaminate + 2-oxoglutarate + O2 = dihydroclavaminate + succinate + CO2 + H2O
show the reaction diagram
dihydroclavaminate + 2-oxoglutarate + O2 = clavaminate + succinate + CO2 + H2O
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
oxidative decarboxylation
-
-
-
-
oxidative cyclization
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
deoxyamidinoproclavaminate,2-oxoglutarate:oxygen oxidoreductase (3-hydroxylating)
Contains nonheme iron. Catalyses three separate oxidative reactions in the pathway for the biosythesis of the beta-lactamase inhibitor clavulanate in Streptomyces clavuligerus. The first step (hydroxylation) is separated from the latter two (oxidative cyclization and desaturation) by the action of EC 3.5.3.22, proclavaminate amidinohydrolase. The three reactions are all catalysed at the same nonheme iron site.
CAS REGISTRY NUMBER
COMMENTARY hide
122799-56-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-oxoglutarate + O2
? + H2O2
show the reaction diagram
deoxyamidinoproclavaminate + 2-oxoglutarate + O2
amidinoproclavaminate + succinate + CO2 + H2O
show the reaction diagram
deoxyguanidinoproclavaminate + 2-oxoglutarate + O2
guanidinoproclavaminate + succinate + CO2 + H2O
show the reaction diagram
dihydroclavaminate + 2-oxoglutarate + O2
clavaminate + succinate + CO2 + H2O
show the reaction diagram
N-alpha-acetyl-L-arginine + 2-oxoglutarate + O2
4-hydroxy-N-alpha-acetyl-L-arginine + succinate + CO2 + H2O
show the reaction diagram
proclavaminate + 2-oxoglutarate + O2
dihydroclavaminate + succinate + CO2 + H2O
show the reaction diagram
(2S,3R)-proclavaminate + 2-oxoglutarate + O2
clavaminate + succinate + CO2 + H2O
show the reaction diagram
-
-
-
-
r
(3S,5S)-dihydroclavaminate + 2-oxoglutarate + O2
(3S,5S)-clavaminate + succinate + CO2 + H2O
show the reaction diagram
the enzyme is involved in clavulanic acid biosynthesis
-
-
?
2-oxoglutarate + O2
? + H2O2
show the reaction diagram
deoxyamidinoproclavaminate + 2-oxoglutarate + O2
amidinoproclavaminate + succinate + CO2 + H2O
show the reaction diagram
deoxyamidinoproclavaminate + 2-oxoglutarate + O2
E-(2S)-5-amino-2(2'-oxoazetidin-1-yl)-pent-3,4-enoate + succinate + CO2 + H2O + ?
show the reaction diagram
-
isozyme CS2
10% of the product is proclavaminate, 90% of the product is E-(2S)-5-amino-2(2'-oxoazetidin-1-yl)-pent-3,4-enoate
?
deoxyguanidinoproclavaminate + 2-oxoglutarate + O2
guanidinoproclavaminate + succinate + CO2 + H2O
show the reaction diagram
dihydroclavaminate + 2-oxoglutarate + O2
clavaminate + succinate + CO2 + H2O
show the reaction diagram
N-alpha-acetyl-L-arginine + 2-oxoglutarate + O2
4-hydroxy-N-alpha-acetyl-L-arginine + succinate + CO2 + H2O
show the reaction diagram
proclavaminate + 2-oxoglutarate + O2
dihydroclavaminate + succinate + CO2 + H2O
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
deoxyamidinoproclavaminate + 2-oxoglutarate + O2
amidinoproclavaminate + succinate + CO2 + H2O
show the reaction diagram
-
-
?
deoxyguanidinoproclavaminate + 2-oxoglutarate + O2
guanidinoproclavaminate + succinate + CO2 + H2O
show the reaction diagram
dihydroclavaminate + 2-oxoglutarate + O2
clavaminate + succinate + CO2 + H2O
show the reaction diagram
proclavaminate + 2-oxoglutarate + O2
dihydroclavaminate + succinate + CO2 + H2O
show the reaction diagram
(3S,5S)-dihydroclavaminate + 2-oxoglutarate + O2
(3S,5S)-clavaminate + succinate + CO2 + H2O
show the reaction diagram
the enzyme is involved in clavulanic acid biosynthesis
-
-
?
deoxyamidinoproclavaminate + 2-oxoglutarate + O2
amidinoproclavaminate + succinate + CO2 + H2O
show the reaction diagram
deoxyguanidinoproclavaminate + 2-oxoglutarate + O2
guanidinoproclavaminate + succinate + CO2 + H2O
show the reaction diagram
dihydroclavaminate + 2-oxoglutarate + O2
clavaminate + succinate + CO2 + H2O
show the reaction diagram
proclavaminate + 2-oxoglutarate + O2
dihydroclavaminate + succinate + CO2 + H2O
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4'-ethynyl proclavaminate
-
noncompetitive
4'-vinyl proclavaminate
-
noncompetitive
4-cyclopropyl proclavaminate
-
noncompetitive
ascorbate
-
inactivation due to release of peroxide from reaction of ascorbate and O2 in absence of proclavaminate, but in presence of Fe2+, t1/2: 50 min, catalase protects
diethyl dicarbonate
-
isozyme CS2, rapid inactivation at pH 6.0, 25°C, t1/2: 1.1 min
N-bromoacetyl-L-arginine
-
isozyme CS2, inactivation, at 7.5 mM half-life of 11.2 min at 30°C, Co2+ competes, substrates protect
N-ethylmaleimide
-
inactivation
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.19
(2S,3R)-proclavaminate
-
pH 7.0, 22°C
0.042
2-oxoglutarate
-
pH 7.0, 22°C
0.0019
Fe2+
-
pH 7.0, 22°C
0.23
N-alpha-acetyl-L-arginine
-
pH 7.0, 22°C
0.13 - 0.22
proclavaminate
0.38
rac-proclavaminate
-
pH 7.0, 22°C
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.765
(2S,3R)-proclavaminate
-
pH 7.0, 40°C
6.4
N-alpha-acetyl-L-arginine
-
pH 7.0, 22°C
0.725
rac-proclavaminate
-
pH 7.0, 40°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
38.3
N-bromoacetyl-L-arginine
-
isozyme CS2, pH 7.0, 30°C
additional information
additional information
-
Ki of 4'-vinyl proclavaminate, 4'-ethynyl proclavaminate, and 4-cyclopropyl proclavaminate is in the range of 2-10 mM
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.4
-
65fold purified enzyme
0.57
-
purified enzyme, 40°C
0.8
-
purified recombinant isozyme CS2
0.86
-
purified recombinant isozyme CS1
additional information
-
activity of wild-type and mutant in different growth media
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
room temperature, assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
CAS2 is classified to the taurine catabolism dioxygenase TauD family with the Pfam accession of PF02668, referred to as subgroup II of the 2-oxoglutarate-Fe(II)-dioxygenase superfamily
evolution
CAS1 is classified to the taurine catabolism dioxygenase TauD family with the Pfam accession of PF02668, referred to as subgroup II of the 2-oxoglutarate-Fe(II)-dioxygenase superfamily
metabolism
the enzyme is involved in clavulanic acid biosynthesis
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
CAS1_STRCL
324
0
35370
Swiss-Prot
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35360
35750
38000
-
CS1, gel filtration
42000
-
CS2, gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
anaerobically, recombinant isozyme CAS1, in complex with Fe2+, 2-oxoglutarate and deoxyguanidinoproclavaminate, hanging drop vapour diffusion method, protein solution: 20 mg/ml, reservoir solution: 0.1 M Tris, pH 7.5, 2 M ammonium sulfate, 10% glycerol, 20°C, treatment with NO under anaerobic conditions, structure determination and analysis
moelcular dynamics simulation, model of the active site
recombinant isozyme CAS1, hanging drop method, 2 M ammonium sulfate, 0.1 M Tris, 21°C, apoform crystals or in complex with Fe2+, N-alpha-acetyl-L-arginine, and the substrates 2-oxoglutarate and proclavaminate, X-ray diffraction structure determination for native and heavy atom derivatives and analysis
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C162L
-
isozyme CAS2, site-directed mutagenesis, same activity in hydroxylation of N-alpha-acetyl-L-arginine as the wild-type enzyme
C200L
-
isozyme CAS2, site-directed mutagenesis, 42% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
C201L
-
isozyme CAS2, site-directed mutagenesis, 40% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
C8L
-
isozyme CAS2, site-directed mutagenesis, 42% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H109L
-
isozyme CAS2, site-directed mutagenesis, 86% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H109Q
-
isozyme CS2, site-directed mutagensis, 83% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
H122L
-
isozyme CAS2, site-directed mutagenesis, below 1% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H122Q
-
isozyme CS2, site-directed mutagensis, 96% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
H131L
-
isozyme CAS2, site-directed mutagenesis, 36% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H131Q
-
isozyme CS2, site-directed mutagensis, 16% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
H145E
-
isozyme CAS2, site-directed mutagenesis, below 1% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H145L
-
isozyme CAS2, site-directed mutagenesis, below 1% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H145Q
H151l
-
isozyme CAS2, site-directed mutagenesis, below 1% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H151Q
-
isozyme CS2, site-directed mutagensis, 10% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
H167L
-
isozyme CAS2, site-directed mutagenesis, 19% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H167Q
-
isozyme CS2, site-directed mutagensis, 95% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
H280L
-
isozyme CAS2, site-directed mutagenesis, 86% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H280Q
-
isozyme CS2, site-directed mutagensis, no activity of clavaminate formation, but slight hydroxylating activity of deoxyguanidinoproclavaminate
H297L
-
isozyme CAS2, site-directed mutagenesis, 3% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
H297Q
-
isozyme CS2, site-directed mutagensis, 65% activity of clavaminate formation compared to the wild-type enzyme, unaltered hydroxylating activity
Q154L
-
isozyme CAS2, site-directed mutagenesis, 23% activity in hydroxylation of N-alpha-acetyl-L-arginine compared to the wild-type enzyme
additional information
-
construction of a disruption mutant of isozyme cas2 by a gene replacement procedure, mutant shows no activity in starch-asparagine medium, but reduced activity, compared to the wild-type, in soy medium which is due to CAS1 isozyme, different regulation of the 2 isozymes concerning nutritional conditions
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Co2+ completely inhibits the enzyme, competitive to Fe2+, but also stabilizes the enzyme against self-inactivation in absence of proclavaminate
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
inactivation due to release of peroxide from reaction of 2-oxoglutarate and O2 in absence of proclavaminate, in presence of Fe2+, t1/2: 5 min, with ascorbate instead of 2-oxoglutarate t1/2: 50 min, catalase protects
-
639270, 639275
inactivation due to release of peroxide from reaction of 2-oxoglutarate and O2 in absence of proclavaminate, in presence of Fe2+, t1/2: 52 s, catalase partially protects
-
639274
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, purified enzyme, frozen in liquid N2, stable for at least several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant isozymes CS1 and CS2 to homogeneity, 10fold
-
recombinant wild-type and mutants of isozyme CS2 from Escherichia coli JM101
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cs2, isozyme CS2, wild-type and mutants, overexpression in Escherichia coli JM101
-
isozymes CAS1 and CAS2 encoded by genes cas1 and cas2, respectively, genetic analysis
-
isozymes CS1 and CS2, overexpression in Escherichia coli JM101
-
Streptomyces venezuelae YJ028 is utilized as the heterologous host for the expression of four structural clavulanic acid biosynthesis genes, which encode carboxyethylarginine synthase (ceas2), beta-lactam synthetase (bls2), clavaminate synthase (cas2), and proclavaminate amidinohydrolase (pah2). The genes are cloned into pIBR25 expression vector containing ermE promoter to generate pBS4. The cas2 gene is also cloned into pSET152 to generate pCas2. It is then integrated into the genome of Streptomyces venezuelae YJ028
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
synthesis
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Townsend, C.A.
New reactions in clavulanic acid biosynthesis
Curr. Opin. Chem. Biol.
6
583-589
2002
Streptomyces clavuligerus
Manually annotated by BRENDA team
Salowe, S.P.; Marsh, E.N.; Townsend, C.A.
Purification and characterization of clavaminate synthase from Streptomyces clavuligerus: an unusual oxidative enzyme in natural product biosynthesis
Biochemistry
29
6499-6508
1990
Streptomyces clavuligerus
Manually annotated by BRENDA team
Salowe, S.P.; Krol, W.J.; Iwata-Reuyl, D.; Townsend, C.A.
Elucidation of the order of oxidations and identification of an intermediate in the multistep clavaminate synthase reaction
Biochemistry
30
2281-2292
1991
Streptomyces clavuligerus
Manually annotated by BRENDA team
Elson, S.W.; Baggaley, K.H.; Holland, S.; Nicholson, N.H.; Sime, J.T.; Woroniecki, S.R.
Studies on the substrate specificity of clavaminic acid synthase and associated enzymes
Bioorg. Med. Chem. Lett.
2
1503-1508
1992
Streptomyces clavuligerus
-
Manually annotated by BRENDA team
Iwata-Reuyl, D.; Basak, A.; Silverman, L.S.; Engle, C.A.; Townsend, C.A.
Synthesis and reaction of potential alternate substrates and mechanism-based inhibitors of clavaminate synthase
J. Nat. Prod.
56
1373-1396
1993
Streptomyces clavuligerus
Manually annotated by BRENDA team
Janc, J.W.; Egan, L.A.; Townsend, C.A.
Purification and characterization of clavaminate synthase from Streptomyces antibioticus. A multifunctional enzyme of clavam biosynthesis
J. Biol. Chem.
270
5399-5404
1995
Streptomyces antibioticus, Streptomyces antibioticus Tu1718, Streptomyces clavuligerus
Manually annotated by BRENDA team
Busby, R.W.; Chang, M.D.T.; Busby, R.C.; Wimp, J.; Townsend, C.A.
Expression and purification of two isoenzymes of clavaminate synthase and initial characterization of the iron binding site. General error analysis in polymerase chain reaction amplification
J. Biol. Chem.
270
4262-4269
1995
Streptomyces clavuligerus
Manually annotated by BRENDA team
Paradkar, A.S.; Jensen, S.E.
Functional analysis of the gene encoding the clavaminate synthase 2 isoenzyme involved in clavulanic acid biosynthesis in Streptomyces clavuligerus
J. Bacteriol.
177
1307-1314
1995
Streptomyces clavuligerus, Streptomyces clavuligerus NRRL 3585
Manually annotated by BRENDA team
Busby, R.W.; Townsend, C.A.
A single monomeric iron center in clavaminate synthase catalyzes three nonsuccessive oxidative transformations
Bioorg. Med. Chem.
4
1059-1064
1996
Streptomyces clavuligerus
Manually annotated by BRENDA team
Baldwin, J.E.; Adlington, R.M.; Bryans, J.S.; Lloyd, M.D.; Sewell, T.J.; Schofield, C.J.; Baggaley, K.H.; Cassels, R.
Chemo-enzymic synthesis of bicyclic gamma-lactams using clavaminic acid synthase
Tetrahedron
53
7011-7020
1997
Streptomyces clavuligerus
-
Manually annotated by BRENDA team
Zhou, J.; Gunsior, M.; Bachmann, B.O.; Townsend, C.A.; Solomon, E.I.
Substrate binding to the alpha-ketoglutarate-dependent non-heme iron enzyme clavaminate synthase 2: coupling mechanism of oxidative decarboxylation and hydroxylation
J. Am. Chem. Soc.
120
13539-13540
1998
Streptomyces clavuligerus
-
Manually annotated by BRENDA team
Lloyd, M.D.; Merritt, K.D.; Lee, V.; Sewell, T.J.; Wha-Son, B.; Baldwin, J.E.; Schofield, C.J.; Elson, S.W.; Baggaley, K.H.; Nicholson, N.H.
Product-substrate engineering by bacteria: studies on clavaminate synthase, a trifunctional dioxygenase
Tetrahedron
55
10201-10220
1999
Streptomyces clavuligerus
-
Manually annotated by BRENDA team
Zhang, Z.; Ren, J.; Stammers, D.K.; Baldwin, J.E.; Harlos, K.; Schofield, C.J.
Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase
Nat. Struct. Biol.
7
127-133
2000
Streptomyces clavuligerus (Q05581)
Manually annotated by BRENDA team
Khaleeli, N.; Busby, R.W.; Townsend, C.A.
Site-directed mutagenesis and biochemical analysis of the endogenous ligands in the ferrous active site of clavaminate synthase. The His-3 variant of the 2-His-1-carboxylate model
Biochemistry
39
8666-8673
2000
Streptomyces clavuligerus
Manually annotated by BRENDA team
Doan, L.X.; Hassan, A.; Lipscomb, S.J.; Dhanda, A.; Zhang, Z.; Schofield, C.J.
Mutagenesis studies on the iron binding ligands of clavaminic acid synthase
Biochem. Biophys. Res. Commun.
279
240-244
2000
Streptomyces clavuligerus
Manually annotated by BRENDA team
Zhou, J.; Kelly, W.L.; Bachmann, B.O.; Gunsior, M.; Townsend, C.A.; Solomon, E.I.
Spectroscopic studies of substrate interactions with clavaminate synthase 2, a multifunctional a-KG-dependent non-heme iron enzyme: correlation with mchanisms and reactivities
J. Am. Chem. Soc.
123
7388-7398
2001
Streptomyces clavuligerus (Q05581)
Manually annotated by BRENDA team
Zhang, Z.; Ren, J.s.; Harlos, K.; McKinnon, C.H.; Clifton, I.J.; Schofield, C.J.
Crystal structure of a clavaminate synthase-Fe(II)-2-oxoglutarate-substrate-NO complex: evidence for metal centred rearrangements
FEBS Lett.
517
7-12
2002
Streptomyces clavuligerus (Q05581)
Manually annotated by BRENDA team
Borowski, T.; de Marothy, S.; Broclawik, E.; Schofield, C.J.; Siegbahn, P.E.
Mechanism for cyclization reaction by clavaminic acid synthase. Insights from modeling studies
Biochemistry
46
3682-3691
2007
Streptomyces clavuligerus (Q05581)
Manually annotated by BRENDA team
Chin, H.; Goh, K.; Teo, K.; Chan, M.; Lee, S.; Ong, L.
Predicting the catalytic sites of Streptomyces clavuligerus deacetylcephalosporin C synthase and clavaminate synthase 2
Afr. J. Microbiol. Res.
5
3357-3366
2011
Streptomyces clavuligerus (Q05581), Streptomyces clavuligerus (Q05582)
-
Manually annotated by BRENDA team
Shrestha, B.; Dhakal, D.; Darsandhari, S.; Pandey, R.; Pokhrel, A.; Jnawali, H.; Sohng, J.
Heterologous production of clavulanic acid intermediates in Streptomyces venezuelae
Biotechnol. Bioprocess Eng.
22
359-365
2017
Streptomyces clavuligerus (Q53939)
-
Manually annotated by BRENDA team