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Information on EC 2.5.1.7 - UDP-N-acetylglucosamine 1-carboxyvinyltransferase and Organism(s) Enterobacter cloacae and UniProt Accession P33038

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Enterobacter cloacae
UNIPROT: P33038 not found.
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The taxonomic range for the selected organisms is: Enterobacter cloacae
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
udp-n-acetylglucosamine enolpyruvyl transferase, mura enzyme, muraa, udp-n-acetylglucosamine 1-carboxyvinyltransferase, udp-n-acetylglucosamine enolpyruvyltransferase, udp-nag enolpyruvyl transferase, udp-n-acetylglucosamine 1-carboxyvinyl-transferase, udp-n-acetylglucosamine 1-carboxyvinyl transferase, udp-n-acetylglucosamine enolpyruvyle transferase, udp-glcnac enolpyruvyl transferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
UDP-N-acetylglucosamine 1-carboxyvinyltransferase
-
UDP-N-acetylglucosamine enolpyruvyl transferase
-
enol-pyruvyltransferase
-
-
enoylpyruvate transferase
-
-
-
-
enoylpyruvatetransferase
-
-
-
-
MurA transferase
-
-
-
-
phosphoenolpyruvate-UDP-acetylglucosamine-3-enolpyruvyltransferase
-
-
-
-
phosphoenolpyruvate:UDP-2-acetamido-2-deoxy-D-glucose 2-enoyl-1-carboxyethyltransferase
-
-
-
-
phosphoenolpyruvate:uridine diphosphate N-acetylglucosamine enolpyruvyltransferase
-
-
-
-
phosphoenolpyruvate:uridine-5'-diphospho-N-acetyl-2-amino-2-deoxyglucose-3-enolpyruvyltransferase
-
-
-
-
phosphopyruvate-uridine diphosphoacetylglucosamine pyruvatetransferase
-
-
-
-
pyruvate-UDP-acetylglucosamine transferase
-
-
-
-
pyruvate-uridine diphospho-N-acetyl-glucosamine transferase
-
-
-
-
pyruvate-uridine diphospho-N-acetylglucosamine transferase
-
-
-
-
pyruvatetransferase, phosphoenolpyruvate-uridine diphosphoacetylglucosamine
-
-
-
-
pyruvic-uridine diphospho-N-acetylglucosaminyltransferase
-
-
-
-
UDP-GlcNAc enolpyruvyl transferase
-
-
UDP-N-acetylglucosamine 1-carboxyvinyl-transferase
UDP-N-acetylglucosamine enolpyruvyl transferase
-
-
UDP-N-acetylglucosamine enolpyruvyltransferase
-
-
UDP-N-acetylglucosamine enoylpyruvyltransferase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
show the reaction diagram
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine = phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
carboxyvinyl group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
phosphoenolpyruvate:UDP-N-acetyl-D-glucosamine 1-carboxyvinyltransferase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9023-27-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
show the reaction diagram
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
UDP-N-acetyl-3-O-(1-carboxyvinyl)-D-glucosamine + phosphate
show the reaction diagram
-
-
-
r
phosphoenol-2-oxobutyrate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetylglucosaminyl-enol-2-oxobutyrate
show the reaction diagram
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
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
phosphoenolpyruvate + UDP-N-acetyl-alpha-D-glucosamine
phosphate + UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine
show the reaction diagram
-
-
-
-
?
phosphoenolpyruvate + UDP-N-acetyl-D-glucosamine
phosphate + UDP-N-acetyl-3-(1-carboxyvinyl)-D-glucosamine
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
not affected by K+, Na+, Mg2+, and Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(S)-2-[2-(naphthalene-1-sulfonylamino)-5-(naphthalene-1-sulfonyloxy)-benzoylamino]-pentanedioic acid
competitive with UDP-N-acetylglucosamine
(S)-2-[2-(naphthalene-1-sulfonylamino)-5-(naphthalene-1-sulfonyloxy)-benzoylamino]-succinic acid
-
1-tuliposide A
potent inhibitor
1-tuliposide B
potent inhibitor
2-oxo-1,3-benzoxathiol-5-yl (3-chlorophenyl)carbamate
-
2-oxo-1,3-benzoxathiol-6-yl benzenesulfonate
-
2-oxo-1,3-benzoxathiol-6-yl methanesulfonate
-
4,7-dichloro-5-hydroxy-1,3-benzoxathiol-2-one
-
5-(prop-2-en-1-yloxy)-1,3-benzoxathiol-2-one
-
5-bromo-2-oxo-1,3-benzoxathiol-6-yl phenyl carbonate
-
5-hydroxy-1,3-benzoxathiol-2-one
-
5-hydroxy-7-(4-methoxyphenyl)-1,3-benzoxathiol-2-one
-
5-hydroxynaphtho[1,2-d][1,3]oxathiol-2-one
-
fosfomycin
HESFWYLPHHQSY
competitive inhibition
pyrazolopyrimidine
reversible inhibitor
RWJ-110192
reversible inhibitor
RWJ-140998
irreversible inhibitor
RWJ-3981
irreversible inhibitor
T6361
competitive inhibition
T6362
terreic acid
irreversible inhibitor
Trypsin
wild-type and mutant C115S, no protection via individually binding of substrates or inhibitor fosfomycin, but via binding of both, the 2 substrates and inhibitor fosfomycin
-
(+)-6-tuliposide B
-
35% residual activity at 0.1 mM
(+)-tulipalin B
-
3.3% residual activity at 0.1 mM
(-)-tulipalin B
-
3.7% residual activity at 0.1 mM
3-Bromopyruvate
-
irreversible, inhibitory effect is increased by UDP-GlcNAc
3-methylidenedihydrofuran-2(3H)-one
-
54% residual activity at 0.1 mM
epi-(+)-6-tuliposide B
-
19% residual activity at 0.1 mM
fosfomycin
iodoacetamide
-
inhibition by alkylation of the active site Cys155, pH-dependent, no alkylation below pH 7.0, maximum alkylation at pH 9.0
iodoacetate
-
-
N-ethylmaleimide
-
-
p-chloromercuribenzoate
-
-
phosphoenol-2-ketovalerate
-
-
UDP-N-acetylmuramyl-L-Ala-D-Glu-meso-alpha,epsilon-diaminopimelic acid
-
inhibitor binding site is distinct from active site
uridine diphospho-N-acetylmuramyl-L-Ala-D-gamma-Glu-meso-alpha,epsilon-diaminopimelic-acid-D-Ala-D-Ala
-
inhibitor binding site is distinct from active site
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
dithiothreitol
included in the assay reaction mixture
thiol groups
-
required for activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0083
phosphoenolpyruvate
pH and temperature not specified in the publication
0.08
UDP-N-acetyl-D-glucosamine
pH and temperature not specified in the publication
0.008 - 0.03
phosphoenolpyruvate
0.08 - 0.46
UDP-GlcNAc
additional information
additional information
-
Km values of mutant enzymes for the substrates
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3
phosphoenolpyruvate
pH and temperature not specified in the publication
3
UDP-N-acetyl-D-glucosamine
pH and temperature not specified in the publication
3
phosphoenolpyruvate
-
wild-type enzyme
3
UDP-GlcNAc
-
wild-type enzyme
additional information
additional information
-
kcat values of mutant enzymes for the substrates
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00036
phosphoenolpyruvate
pH and temperature not specified in the publication
0.0000375
UDP-N-acetyl-D-glucosamine
pH and temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016
T6362
20°C, pH 8.0
1.7
phosphoenol-2-ketovalerate
-
-
4.9 - 6.6
UDP-N-acetylmuramyl-L-Ala-D-Glu-meso-alpha,epsilon-diaminopimelic acid
-
-
0.8
uridine diphospho-N-acetylmuramyl-L-Ala-D-gamma-Glu-meso-alpha,epsilon-diaminopimelic-acid-D-Ala-D-Ala
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.1 - 0.12
-
partially purified enzyme
0.27
-
purified enzyme
1.8
-
purified native enzyme
1.9
-
purified enzyme
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
determination of pKa value for Cys115: 8.3
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
the enzyme catalyzes the first committed step in the biosynthesis of peptidoglycan, an integral and essential component of the bacterial cell wall
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
44780
electrospray ionization-mass spectrometry
34000
-
gel filtration
37000
-
nondenaturing PAGE
41000
-
1 * 41000, SDS-PAGE
42100
-
42100, SDS-PAGE
44780
-
MW deduced from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 44700, SDS-PAGE
monomer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
at 19°C, from 10 mM MES, pH 6.4, 10% (w/v) polyethylene glycol 20000, in the presence of 5 mM UDP-N-acetyl-D-glucosamine and 5 mM phosphoenolpyruvate
in complex with inhibitor T6361
in complex with substrates, hanging drop vapor diffusion method, using 0.1 M Bis-Tris (pH 5.5), 0.2 M NH4OAc, 25% (w/v) PEG 3350
crystallization of substrate-free enzyme, two-domain structure with an unusual fold, inside out alpha/beta barrel, which is built up from the 6fold repetititon of one folding unit, structure analysis
-
mutant D305A, in presence of phosphoenolpyruvate and UDP-N-acetyl-D-glucosamine
-
X-ray structure analysis of ligated and unligated MurA
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C115D
the mutant enzyme lacks the ability to react with phosphoenolpyruvate covalently
C115S
K22V/R120K
no residual activity, heat capacity changes are markedly redcued
K22V/R120V
no residual activity
R120K
less than 0.05% of wild-type activity, heat capacity changes are markedly redcued
C251S
-
site-directed mutagenesis, Cys251 is not involved in the catalysis, unaltered biochemical properties
C354S
-
site-directed mutagenesis, Cys354 is not involved in the catalysis, unaltered biochemical properties
C381S
-
site-directed mutagenesis, Cys381 is not involved in the catalysis, unaltered biochemical properties
D305A
D305C
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity
D305E
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, 0.1% activity compared to the wild-type
D305H
-
site-directed mutagenesis, weaker binding of UDP-GlcNAc, no activity, fosfomycin is not covalently attached to Cys115
N23A
-
site-directed mutagenesis, reduced activity, 20fold higher apparent dissociation constant for fosfomycin compared to wild-type
N23S
-
site-directed mutagenesis, reduced activity, 200fold higher apparent dissociation constant for fosfomycin compared to wild-type
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, loss of activity after 1 week
-
0°C or -20°C, 0.2 mg/ml DTT, 40% loss of activity after 2 weeks
-
4°C, in 80% ammonium sulfate, loss of activity after 1 week
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, phenyl-Sepharose column chromatography, Q-Sepharose column chromatography, Superdex 200 gel filtration, and Sephadex G-25 gel filtration
recombinant from Escherichia coli
recombinant wild-type and mutants from Escherichia coli
covalent adduct of enzyme and phosphoenolpyruvate
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination, functional overexpression in Escherichia coli strain JM105
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli STBL2-DE3 cells
expression of wild-type and mutants in Escherichia coli
DNA and amino acid sequence determination, functional overexpression in Escherichia coli strain JM105
-
expressed in Escherichia coli BL21 cells
-
expression of wild-type and mutants in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Gunetileke, K.G.; Anwar, R.A.
Biosynthesis of uridine diphospho-N-acetylmuramic acid. II. Purification and properties of pyruvate-uridine diphospho-N-acetylglucosamine transferase and characterization of uridine diphospho-N-acetylenopyruvylglucosamine
J. Biol. Chem.
243
5770-5778
1968
Enterobacter cloacae, Enterobacter cloacae NRC 492
Manually annotated by BRENDA team
Zemell, R.I.; Anwar, R.A.
Pyruvate-uridine diphospho-N-acetylglucosamine transferase. Purification to homogeneity and feedback inhibition
J. Biol. Chem.
250
3185-3192
1975
Enterobacter cloacae
Manually annotated by BRENDA team
Zemell, R.I.; Anwar, R.A.
Mechanism of pyruvate-uridine diphospho-N-acetylglucosamine transferase. Evidence for an enzyme-enolpyruvate intermediate
J. Biol. Chem.
250
4959-4964
1975
Enterobacter cloacae
Manually annotated by BRENDA team
Wanke, C.; Falchetto, R.; Amrhein, N.
The UDP-N-acetylglucosamine 1-carboxyvinyl-transferase of Enterobacter cloacae. Molecular cloning, sequencing of the gene and overexpression of the enzyme
FEBS Lett.
301
271-276
1992
Enterobacter cloacae, Enterobacter cloacae DSM 30054
Manually annotated by BRENDA team
Anwar, R.A.; Vlaovic, M.
Effect of phosphoenolpyruvate analogs on the activity of enoylpyruvate transferase and the effect of UDP-N-acetylglucosamine on the reactivity of the active site SH group
Biochim. Biophys. Acta
616
389-394
1980
Enterobacter cloacae
Manually annotated by BRENDA team
Kim, D.H.; Lees, W.J.; Kempsell, K.E.; Lane, W.S.; Duncan, K.; Walsh, C.T.
Characterization of a Cys115 to Asp substitution in the Escherichia coli cell wall biosynthetic enzyme UDP-GlcNAc enolpyruvyl transferase (MurA) that confers resistance to inactivation by the antibiotic fosfomycin
Biochemistry
35
4923-4928
1996
Enterobacter cloacae, Escherichia coli, Escherichia coli MurA
Manually annotated by BRENDA team
Schoenbrunn, E.; Sack, S.; Eschenburg, S.; Perrakis, A.; Krekel, F.; Amrhein, N.; Mandelkow, E.
Crystal structure of UDP-N-acetylglucosamine enolpyruvyltransferase, the target of the antibiotic fosfomycin
Structure
4
1065-1075
1996
Enterobacter cloacae
Manually annotated by BRENDA team
Schonbrunn, E.; Svergun, D.I.; Amrhein, N.; Koch, M.H.J.
Studies on the conformational changes in the bacterial cell wall biosynthetic enzyme UDP-N-acetylglucosamine enolpyruvyltransferase (MurA)
Eur. J. Biochem.
253
406-412
1998
Enterobacter cloacae, Enterobacter cloacae DSM 30054
Manually annotated by BRENDA team
Krekel, F.; Oecking, C.; Amrhein, N.; Macheroux, P.
Substrate and inhibitor-induced conformational changes in the structurally related enzymes UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate 3-phosphate synthase (EPSPS)
Biochemistry
38
8864-8878
1999
Enterobacter cloacae (P33038), Enterobacter cloacae DSM 30054 (P33038)
Manually annotated by BRENDA team
Samland, A.K.; Amrhein, N.; Macheroux, P.
Lysine 22 in UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae is crucial for enzymatic activity and the formation of covalent adducts with the substrate phosphoenolpyruvate and the antibiotic fosfomycin
Biochemistry
38
13162-13169
1999
Enterobacter cloacae (P33038), Enterobacter cloacae, Enterobacter cloacae DSM 30054 (P33038)
Manually annotated by BRENDA team
Krekel, F.; Samland, A.K.; Macheroux, P.; Amrhein, N.; Evans, J.N.S.
Determination of the pKa value of C115 in MurA (UDP-N-acetylglucosamine enolpyruvyltransferase) from Enterobacter cloacae
Biochemistry
39
12671-12677
2000
Enterobacter cloacae, Enterobacter cloacae DSM 30054
Manually annotated by BRENDA team
Samland, A.K.; Jelesarov, I.; Kuhn, R.; Amrhein, N.; Macheroux, P.
Thermodynamic characterization of ligand-induced conformational changes in UDP-N-acetylglucosamine enolpyruvyl transferase
Biochemistry
40
9950-9956
2001
Enterobacter cloacae (P33038), Enterobacter cloacae DSM 30054 (P33038)
Manually annotated by BRENDA team
Samland, A.K.; Etezady-Esfarjani, T.; Amrhein, N.; Macheroux, P.
Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae
Biochemistry
40
1550-1559
2001
Enterobacter cloacae, Enterobacter cloacae DSM 30054
Manually annotated by BRENDA team
Thomas, A.M.; Ginj, C.; Jelesarov, I.; Amrhein, N.; Macheroux, P.
Role of K22 and R120 in the covalent binding of the antibiotic fosfomycin and the substrate-induced conformational change in UDP-N-acetylglucosamine enolpyruvyl transferase
Eur. J. Biochem.
271
2682-2690
2004
Enterobacter cloacae (P33038)
Manually annotated by BRENDA team
Eschenburg, S.; Kabsch, W.; Healy, M.L.; Schonbrunn, E.
A new view of the mechanisms of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) and 5-enolpyruvylshikimate-3-phosphate synthase (AroA) derived from X-ray structures of their tetrahedral reaction intermediate states
J. Biol. Chem.
278
49215-49222
2003
Enterobacter cloacae
Manually annotated by BRENDA team
Eschenburg, S.; Priestman, M.A.; Abdul-Latif, F.A.; Delachaume, C.; Fassy, F.; Schonbrunn, E.
A novel inhibitor that suspends the induced fit mechanism of UDP-N-acetylglucosamine enolpyruvyl transferase (MurA)
J. Biol. Chem.
280
14070-14075
2005
Enterobacter cloacae (P33038)
Manually annotated by BRENDA team
Eschenburg, S.; Priestman, M.; Schoenbrunn, E.
Evidence that the fosfomycin target Cys115 in UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) is essential for product release
J. Biol. Chem.
280
3757-3763
2005
Enterobacter cloacae (P33038), Enterobacter cloacae
Manually annotated by BRENDA team
Klein, C.D.; Bachelier, A.
Molecular modeling and bioinformatical analysis of the antibacterial target enzyme MurA from a drug design perspective
J. Comput. Aided Mol. Des.
20
621-628
2006
Enterobacter cloacae, Escherichia coli
Manually annotated by BRENDA team
Gautam, A.; Rishi, P.; Tewari, R.
UDP-N-acetylglucosamine enolpyruvyl transferase as a potential target for antibacterial chemotherapy: recent developments
Appl. Microbiol. Biotechnol.
92
211-225
2011
Enterobacter cloacae (P33038), Escherichia coli (P0A749), Mycobacterium tuberculosis (P9WJM1), Mycobacterium tuberculosis H37Rv (P9WJM1), Pseudomonas aeruginosa, Staphylococcus aureus, Streptococcus pneumoniae
Manually annotated by BRENDA team
Zhu, J.Y.; Yang, Y.; Han, H.; Betzi, S.; Olesen, S.H.; Marsilio, F.; Schoenbrunn, E.
Functional consequence of covalent reaction of phosphoenolpyruvate with UDP-N-acetylglucosamine 1-carboxyvinyltransferase (MurA)
J. Biol. Chem.
287
12657-12667
2012
Enterobacter cloacae (P33038)
Manually annotated by BRENDA team
Shigetomi, K.; Olesen, S.H.; Yang, Y.; Mitsuhashi, S.; Schoenbrunn, E.; Ubukata, M.
MurA as a primary target of tulipalin B and 6-tuliposide B
Biosci. Biotechnol. Biochem.
77
2517-2519
2013
Enterobacter cloacae, Escherichia coli
Manually annotated by BRENDA team