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Information on EC 4.1.3.27 - anthranilate synthase and Organism(s) Serratia marcescens and UniProt Accession P00897

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EC Tree
     4 Lyases
         4.1 Carbon-carbon lyases
             4.1.3 Oxo-acid-lyases
                4.1.3.27 anthranilate synthase
IUBMB Comments
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase ), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)]. The native enzyme in the complex uses either glutamine or, less efficiently, NH3. The enzyme separated from the complex uses NH3 only.
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This record set is specific for:
Serratia marcescens
UNIPROT: P00897 not found.
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Word Map
The taxonomic range for the selected organisms is: Serratia marcescens
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
anthranilate synthase, anthranilate synthetase, oasa1d, oasa1, oasa2, phnab, anthranilate synthase component i, trped, caasa1, caasa2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
anthranilate synthase
anthranilate synthetase
-
-
-
-
chorismate lyase
-
-
-
-
Glutamine amido-transferase
-
-
-
-
Glutamine amidotransferase
-
-
-
-
synthase, anthranilate
-
-
-
-
synthetase, anthranilate
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
chorismate + L-glutamine = anthranilate + pyruvate + L-glutamate
show the reaction diagram
mechanism
SYSTEMATIC NAME
IUBMB Comments
chorismate pyruvate-lyase (amino-accepting; anthranilate-forming)
In some organisms, this enzyme is part of a multifunctional protein, together with one or more other components of the system for the biosynthesis of tryptophan [EC 2.4.2.18 (anthranilate phosphoribosyltransferase ), EC 4.1.1.48 (indole-3-glycerol-phosphate synthase), EC 4.2.1.20 (tryptophan synthase) and EC 5.3.1.24 (phosphoribosylanthranilate isomerase)]. The native enzyme in the complex uses either glutamine or, less efficiently, NH3. The enzyme separated from the complex uses NH3 only.
CAS REGISTRY NUMBER
COMMENTARY hide
9031-59-8
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
chorismate + L-Gln
anthranilate + pyruvate + L-glutamate
show the reaction diagram
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
chorismate + NH4+
?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
glutaminase activity
-
-
?
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
chorismate + L-glutamine
anthranilate + pyruvate + L-glutamate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
-
required for activity
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(1R,4R,5S,6S)-4-[(1-carboxyethenyl)oxy]-5-hydroxy-7-oxabicyclo[4.1.0]hept-2-ene-2-carboxylic acid
-
-
(3R,4R)-3,4-dihydroxycyclohexa-1,5-diene-1-carboxylic acid
-
-
(3R,4R)-3-azido-4-hydroxycyclohexa-1,5-diene-1-carboxylic acid
-
-
(3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxy-6-methylidenecyclohex-1-ene-1-carboxylic acid
-
-
(3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(3S)-3-[(1-carboxyethenyl)oxy]cyclohepta-1,6-diene-1-carboxylic acid
-
-
(4R,5R)-5-(carboxymethoxy)-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(1R)-1-carboxyethoxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(1S)-1-carboxyethoxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(4R,5R)-5-[(2-carboxyprop-2-en-1-yl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
-
(R)-3-(1-carboxy-ethoxy)benzoic acid
-
-
(S)-3-(1-carboxy-ethoxy)benzoic acid
-
-
1-(1-carboxy-ethyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
-
1-(1-carboxy-ethyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
-
1-(1-carboxyethyl)-2-oxo-1,2-dihydropyridine-4-carboxylic acid
-
-
1-(1-carboxyethyl)-6-oxo-1,6-dihydropyridine-3-carboxylic acid
-
-
1-(2-carboxy-allyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
-
1-(2-carboxy-allyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
-
1-(2-carboxyprop-2-en-1-yl)-2-oxo-1,2-dihydropyridine-4-carboxylic acid
-
-
1-(2-carboxyprop-2-en-1-yl)-6-oxo-1,6-dihydropyridine-3-carboxylic acid
-
-
1-(carboxymethyl)-6-oxo-1,6-dihydropyridine-3-carboxylic acid
-
-
1-carboxymethyl -6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
-
2-(1-carboxy-ethylamino)-isonicotinate
-
-
2-(carboxymethyl-amino)-isonicotinate
-
-
2-amino-3-(1-carboxyethoxy)benzoic acid
-
-
2-[(1-carboxyethyl)amino]pyridine-4-carboxylic acid
-
-
2-[(carboxymethyl)amino]pyridine-4-carboxylic acid
-
-
2-[[(1R,6R)-3-bromo-6-hydroxycyclohexa-2,4-dien-1-yl]oxy]prop-2-enoic acid
-
-
3-(1-carboxy-ethoxy)-4-hydroxymethyl benzoic acid
-
-
3-(1-carboxy-ethoxy)-4-mercaptomethyl benzoic acid
-
-
3-(1-carboxy-ethoxy)-4-methyl benzoic acid
-
-
3-(1-carboxyethoxy)-2-hydroxybenzoic acid
-
-
3-(1-carboxyethoxy)-2-nitrobenzoic acid
-
-
3-(1-carboxyethoxy)-4,5-dihydroxybenzoic acid
-
-
3-(1-carboxyethoxy)-4-(hydroxymethyl)benzoic acid
-
-
3-(1-carboxyethoxy)-4-(sulfanylmethyl)benzoic acid
-
-
3-(1-carboxyethoxy)-4-hydroxybenzoic acid
-
-
3-(1-carboxyethoxy)-4-methoxybenzoic acid
-
-
3-(1-carboxyethoxy)-4-methylbenzoic acid
-
-
3-(1-carboxyethoxy)benzoic acid
-
-
3-[(1-carboxyethenyl)oxy]-4,5-dihydroxybenzoic acid
-
-
3-[(2-carboxyprop-2-en-1-yl)oxy]-4,5-dihydroxybenzoic acid
-
-
4-(azidomethyl)-3-(1-carboxyethoxy)benzoic acid
-
-
4-amino-3-(1-carboxyethoxy)benzoic acid
-
-
4-amino-3-[(1-carboxyethyl)amino]benzoic acid
-
-
4-aminomethyl-3-(1-carboxy-ethoxy)benzoate
-
-
4-azidomethyl-3-(1-carboxy-ethoxy)benzoic acid
-
-
6-diazo-5-oxo-L-norleucine
-
inhibition of Gln-dependent activity, no inactivation of NH4+-dependent activity
iodoacetamide
-
inhibition of Gln-dependent activity, no inactivation of NH4+-dependent activity
L-Trp
tryptophan
-
-
[(3R,4R)-3-[(1-carboxyethenyl)oxy]-4-hydroxycyclohexa-1,5-dien-1-yl]phosphonate
-
-
[4-carboxy-2-(1-carboxyethoxy)phenyl]methanaminium
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0031 - 0.018
chorismate
0.33 - 0.5
Gln
5.9 - 10
NH4+
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
5.6
chorismate
-
pH 7.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
(3S)-3-[(1-carboxyethenyl)oxy]cyclohepta-1,6-diene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.29
(4R,5R)-5-[(1-carboxyethenyl)oxy]-4-hydroxycyclohex-1-ene-1-carboxylic acid
-
pH and temperature not specified in the publication
0.0036
(R)-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25°C
0.0019
(S)-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25°C
0.041
1-(1-carboxy-ethyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
pH 7.0, 25°C
0.0053
1-(1-carboxy-ethyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25°C
0.059
1-(2-carboxy-allyl)-2-oxo-1,2-dihydro-pyridine-4-carboxylate
-
pH 7.0, 25°C
0.12
1-(2-carboxy-allyl)-6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25°C
0.1
1-carboxymethyl -6-oxo-1,6-dihydro-pyridine-3-carboxylate
-
pH 7.0, 25°C
0.05
2-(1-carboxy-ethylamino)-isonicotinate
-
pH 7.0, 25°C
0.094
2-(carboxymethyl-amino)-isonicotinate
-
pH 7.0, 25°C
0.024
3-(1-carboxy-ethoxy)-4-hydroxymethyl benzoic acid
-
pH 7.0, 25°C
0.021
3-(1-carboxy-ethoxy)-4-mercaptomethyl benzoic acid
-
pH 7.0, 25°C
0.026
3-(1-carboxy-ethoxy)-4-methyl benzoic acid
-
pH 7.0, 25°C
0.028
3-(1-carboxyethoxy)-4,5-dihydroxybenzoic acid
-
pH and temperature not specified in the publication
0.0029 - 0.03
3-(1-carboxyethoxy)-4-hydroxybenzoic acid
0.025
3-(1-carboxyethoxy)-4-methoxybenzoic acid
-
pH 7.0, 25°C
0.23
3-[(1-carboxyethenyl)oxy]-4,5-dihydroxybenzoic acid
-
pH and temperature not specified in the publication
0.09
3-[(2-carboxyprop-2-en-1-yl)oxy]-4,5-dihydroxybenzoic acid
-
pH and temperature not specified in the publication
0.043
4-amino-3-(1-carboxyethoxy)benzoic acid
-
pH 7.0, 25°C
0.023
4-aminomethyl-3-(1-carboxy-ethoxy)benzoate
-
pH 7.0, 25°C
0.021
4-azidomethyl-3-(1-carboxy-ethoxy)benzoic acid
-
pH 7.0, 25°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 8
-
about 75% of maximal activity, Gln-dependent activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
TRPG_SERMA
193
0
20868
Swiss-Prot
-
TRPE_SERMA
519
0
57658
Swiss-Prot
-
A0A0G3STW7_SERMA
520
0
57071
TrEMBL
-
A0A0G8B3J0_SERMA
520
0
57120
TrEMBL
-
A0A221FVM3_SERMA
191
0
21199
TrEMBL
-
A0A379ZDG6_SERMA
520
0
57164
TrEMBL
-
A0A6M5HWJ6_SERMA
520
0
57148
TrEMBL
-
A0A221DQR8_SERMA
520
0
57089
TrEMBL
-
A0A656VJQ5_SERMA
520
0
57218
TrEMBL
-
A0A1Q4NU78_SERMA
520
0
57158
TrEMBL
-
A0A8E2QUH4_SERMA
520
0
57150
TrEMBL
-
A0A542BZT8_SERMA
520
0
57189
TrEMBL
-
A0A0P0QF85_SERMA
520
0
57219
TrEMBL
-
A0A7D5XV77_SERMA
520
0
57104
TrEMBL
-
A0A1C3HEF5_SERMA
520
0
57089
TrEMBL
-
A0A2V4FP93_SERMA
520
0
57091
TrEMBL
-
A0A7I0PQE2_SERMA
520
0
57111
TrEMBL
-
A0A5C7CJM2_SERMA
520
0
57134
TrEMBL
-
A0A0G3SNS4_SERMA
191
0
21166
TrEMBL
-
A0A3E2EJQ7_SERMA
193
0
20933
TrEMBL
-
A0A8D6QWD1_SERMA
520
0
57059
TrEMBL
-
A0A2V4G9H1_SERMA
191
0
21185
TrEMBL
-
A0A8F8A6J7_SERMA
520
0
57009
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
140000
-
sucrose density gradient centrifugation
141000
-
sucrose density gradient centrifugation
150000
-
gel filtration
20956
-
2 * 20956 + 2 * 60000
21000
-
ASI, ASII, 2 * 21000 + 2 * 60000, SDS-PAGE
60000
additional information
-
anthranilate synthetase component II has a MW of 21684 Da, determined by amino acid sequence analysis after separation of the two protein components
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetramer
additional information
-
subunit ASI catalyzes NH4+-dependent synthesis of anthranilate. Gln is not a substrate for ASI. ASII provides Gln-amide transfer function
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with chorismate, glutamine and glutamate and in complex with L-tryptophan
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
2°C or -10°C, activity declines to 3400 or 4000 units per mg and remains constant for several months
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
immobilized metal ion affinity chromatography (Ni2+)
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged veresion expressed in Escherichia coli C41(DE3)
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Robb, F.; Hutchinson, M.A.; Belser, W.L.
Anthranilate synthetase. Some physical and kinetic properties of the enzyme from Serratia marcescens
J. Biol. Chem.
246
6908-6912
1971
Serratia marcescens
Manually annotated by BRENDA team
Zalkin, H.; Hwang, L.H.
Anthranilate synthetase from Serratia marcescens
J. Biol. Chem.
246
6899-6907
1971
Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens
-
Manually annotated by BRENDA team
Zalkin, H.
Anthranilate synthetase
Adv. Enzymol. Relat. Areas Mol. Biol.
38
1-39
1973
Klebsiella aerogenes, Aspergillus nidulans, Bacillus subtilis, Saccharomyces cerevisiae, Chromobacterium violaceum, Delftia acidovorans, Comamonas testosteroni, Escherichia coli, Neurospora crassa, Pseudomonas aeruginosa, Pseudomonas putida, Salmonella enterica subsp. enterica serovar Typhimurium, Serratia marcescens
Manually annotated by BRENDA team
Tso, J.Y.; Hermodson, M.A.; Zalkin, H.
Primary structure of Serratia marcescens anthranilate synthase component II
J. Biol. Chem.
255
1451-1457
1980
Serratia marcescens
Manually annotated by BRENDA team
Zalkin, H.
Anthranilate synthase
Methods Enzymol.
113
287-292
1985
Serratia marcescens, Serratia marcescens HY150
Manually annotated by BRENDA team
Spraggon, G.; Kim, C.; Nguyen-Huu, X.; Yee, M.C.; Yanofsky, C.; Mills, S.E.
The structures of anthranilate synthase of Serratia marcescens crystallized in the presence of (i) its substrates, chorismate and glutamine, and a product, glutamate, and (ii) its end-product inhibitor, L-tryptophan
Proc. Natl. Acad. Sci. USA
98
6021-6026
2001
Serratia marcescens (P00897 and P00500), Serratia marcescens
Manually annotated by BRENDA team
Payne, R.J.; Bulloch, E.M.; Abell, A.D.; Abell, C.
Design and synthesis of aromatic inhibitors of anthranilate synthase
Org. Biomol. Chem.
3
3629-3635
2005
Serratia marcescens
Manually annotated by BRENDA team
Payne, R.J.; Bulloch, E.M.; Kerbarh, O.; Abell, C.
Inhibition of chorismate-utilising enzymes by 2-amino-4-carboxypyridine and 4-carboxypyridone and 5-carboxypyridone analogues
Org. Biomol. Chem.
8
3534-3542
2010
Serratia marcescens
Manually annotated by BRENDA team
Svarcova, M.; Kratky, M.; Vinsova, J.
Investigation of potential inhibitors of chorismate-utilizing enzymes
Curr. Med. Chem.
22
1383-1399
2015
Serratia marcescens
Manually annotated by BRENDA team
Srivastava, A.; Sinha, S.
Uncoupling of an ammonia channel as a mechanism of allosteric inhibition in anthranilate synthase of Serratia marcescens dynamic and graph theoretical analysis
Mol. Biosyst.
13
142-155
2017
Serratia marcescens
Manually annotated by BRENDA team