Any feedback?
Information on EC 2.6.1.85 - aminodeoxychorismate synthase and Organism(s) Escherichia coli and UniProt Accession P05041
for references in articles please use BRENDA:EC2.6.1.85Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.6.1.85 aminodeoxychorismate synthaseIUBMB Comments
The enzyme is composed of two parts, a glutaminase (PabA in Escherichia coli) and an aminotransferase (PabB). In the absence of PabA and glutamine (but in the presence of Mg2+), PabB can convert ammonia and chorismate into 4-amino-4-deoxychorismate. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. In many organisms, including plants, the genes encoding the two proteins have fused to encode a single bifunctional protein. This enzyme is coupled with EC 4.1.3.38, aminodeoxychorismate lyase, to form 4-aminobenzoate. cf. EC 2.6.1.123, 4-amino-4-deoxychorismate synthase (2-amino-4-deoxychorismate-forming).
Specify your search results
Word Map
- 2.6.1.85
- folate
- p-aminobenzoate
- anthranilate
- isochorismate
-
chorismate-utilizing
-
para-aminobenzoic
-
amidotransferase
- shikimate
-
macrolactone
-
biofortification
- enterobactin
- candicidin
- biotechnology
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
hide(Overall reactions are displayed. Show all >>)
Synonyms
aminodeoxychorismate synthase, pabab, 4-amino-4-deoxychorismate synthase, adc synthase, pvadcs, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-amino-4-deoxychorismate synthase
-
-
-
-
ADC synthase
-
-
-
-
PabB
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
the enzyme is composed of two parts, PabA and PabB
-
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
association of PabA and PabB is greatly enhanced by 5 mM glutamine and greatly reduced at cold temperatures
-
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
in the absence of PabA and glutamine, PabB converts ammonia and chorismate into 4-amino-4-deoxychorismate (in the presence of Mg2+)
-
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
non linear production of PABA in the ADC synthase-ADC lyase-coupled reaction system, at different glutamine and chorismate concentrations, with limiting PabB
-
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
mechanism includes nucleophile addition to C2 of chorismate in an SN2'' process
-
chorismate + L-glutamine = 4-amino-4-deoxychorismate + L-glutamate
omega-amino group of K274 adds to chorismate at C2, leading to elimination of the C4 hydroxyl in an SN2'' displacement reaction. After attack of ammonia to intermediate, another SN2'' displacement expels K274 and forms aminodeoxychorismate
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
amino group transfer
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
chorismate:L-glutamine aminotransferase
The enzyme is composed of two parts, a glutaminase (PabA in Escherichia coli) and an aminotransferase (PabB). In the absence of PabA and glutamine (but in the presence of Mg2+), PabB can convert ammonia and chorismate into 4-amino-4-deoxychorismate. PabA converts glutamine into glutamate only in the presence of stoichiometric amounts of PabB. In many organisms, including plants, the genes encoding the two proteins have fused to encode a single bifunctional protein. This enzyme is coupled with EC 4.1.3.38, aminodeoxychorismate lyase, to form 4-aminobenzoate. cf. EC 2.6.1.123, 4-amino-4-deoxychorismate synthase (2-amino-4-deoxychorismate-forming).
CAS REGISTRY NUMBER
COMMENTARY
132264-37-0
-
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
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
commited step in PABA biosynthesis
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
r
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
commited step in PABA biosynthesis
-
?
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
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
commited step in PABA biosynthesis
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
?
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
-
-
r
chorismate + L-glutamine
4-amino-4-deoxychorismate + L-glutamate
-
commited step in PABA biosynthesis
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5R,6R)-4-ammonio-5-((1-carboxylatovinyl)oxy)-6-hydroxycyclohex-1-ene-1-carboxylate
-
transition-state analogue, competitive
additional information
-
not inhibited by ATP, AMP, dAMP, guanosine, GMP, dGMP, GTP, deoxyguanosine, dTMP, serine, glycine, tyrosine, methionine, p-hydroxybenzoate, PABA, sulfanilamide
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.6
L-glutamine
-
mutant K213A/Q147K amidotransferase activity, pH 8.0, 25°C
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0007 - 0.0056
(5R,6R)-4-ammonio-5-((1-carboxylatovinyl)oxy)-6-hydroxycyclohex-1-ene-1-carboxylate
0.0007
(5R,6R)-4-ammonio-5-((1-carboxylatovinyl)oxy)-6-hydroxycyclohex-1-ene-1-carboxylate
-
mutant K274A, pH 8.5, 25°C
0.0056
(5R,6R)-4-ammonio-5-((1-carboxylatovinyl)oxy)-6-hydroxycyclohex-1-ene-1-carboxylate
-
wild-type, pH 8.5, 25°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
-
heterodimer of chorismate aminating subunit and glutamine amidotransferase subunit. Mass of glutamine amidotransferase subunit is 50969 Da, as determined by electrospray mass spectrometry
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K213A
-
subunit PabB, numbering used is based on the EntC protein from Escherichia coli, reduced activity
K213A/Q147K
-
subunit PabB, numbering used is based on the EntC protein from Escherichia coli, strongly reduced activity
K274A/L277R/D299E/N303H/I306L/F334Y/C391G
mutant displaying anthranilate synthase activity, the kcat/Kchoris value for anthranilate formation is 25% of the wild-type aminodeoxychorismate synthase value for 4-amino-4-deoxychorismate production
N213V/L214P/K274A/L277R/D299E/N303H/F334Y/P363N/I367L/C391G/G425A
mutant displaying anthranilate synthase activity, is able to produce both 2-amino-2-deoxyisochorismate and anthranilate
N213V/L214P/R259S/K274A/L277R/N303H/F334Y/S366T/C391G/G254A
mutant displaying anthranilate synthase activity, is able to produce both 2-amino-2-deoxyisochorismate and anthranilate
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80º, 50 mM MOPS, 50 mM KCl, 0.1 mM EDTA, 2 mM DTT, 5 mM MgCl, pH 7.6
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
chromatography on Poros HQ50, HS20 cation exchange chromatography and chromatography on hydroxyapatite
protamine sulfate precipitation, ammonium sulfate fractionation, chromatography on Sephacryl S-200, chromatography on DEAE-Sephacel and chromatography on dye-agarose
-
streptomycin sulfate precipitation, ammonium sulfate fractionation, chromatography on DEAE-cellulose
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
biotechnology
conversion of aminodeoxychorismate synthase into anthranilate synthase employing a bioinformatics method for predicting mutations required to functionally interconvert homologous enzymes. Complementation of an anthranilate synthase-deficient strain of Escherichia coli grown on minimal medium leads to several aminodeoxychorismate synthase mutants that allow growth in 6 days compared to 2 days for wild-type anthranilate synthase. The purified mutant enzymes catalyze the conversion of chorismate to anthranilate at rates that are about 50% of the rate of wild-type aminodeoxychorismate synthase-catalyzed conversion of chorismate to aminodeoxychorismate. The residues mutated do not contact the substrate
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ye, Q.Z.; Liu, J.; Walsh, C.T.
p-Aminobenzoate synthesis in Escherichia coli: purification and characterization of PabB as aminodeoxychorismate synthase and enzyme X as aminodeoxychorismate lyase
Proc. Natl. Acad. Sci. USA
87
9391-9395
1990
Escherichia coli
Viswanathan, V.K.; Green, J.M.; Nicholas, B.P.
Kinetic characterization of 4-amino 4-deoxychorismate synthase from Escherichia coli
J. Bacteriol.
177
5918-5923
1995
Escherichia coli
Rayl, E.A.; Green, J.M.; Nichols, B.P.
Escherichia coli aminodeoxychorismate synthase: analysis of pabB mutations affecting catalysis and subunit association
Biochim. Biophys. Acta
1295
81-88
1996
Escherichia coli
Parsons, J.F.; Jensen, P.Y.; Pachikara, A.S.; Howard, A.J.; Eisenstein, E.; Ladner, J.E.
Structure of Escherichia coli Aminodeoxychorismate Synthase: architectural conservation and diversity in chorismate-utilizing enzymes
Biochemistry
41
2198-2208
2002
Escherichia coli (P05041), Escherichia coli
He, Z.; Stigers Lavoie, K.D.; Bartlett, P.A.; Toney, M.D.
Conservation of mechanism in three chorismate-utilizing enzymes
J. Am. Chem. Soc.
126
2378-2385
2004
Escherichia coli
Bulloch, E.M.M.; Jones, M.A.; Parker, E.J.; Osborne, A.P.; Stephens, E.; Davies, G.M.; Coggins, J.R.; Abell, C.
Identification of 4-amino-4-deoxychorismate synthase as the molecular target for the antimicrobial action of (6S)-6-fluoroshikimate
J. Am. Chem. Soc.
126
9912-9913
2004
Escherichia coli
Ziebart, K.T.; Toney, M.D.
Nucleophile specificity in anthranilate synthase, aminodeoxychorismate synthase, isochorismate synthase, and salicylate synthase
Biochemistry
49
2851-2859
2010
Escherichia coli
Culbertson, J.E.; Chung, D.h.; Ziebart, K.T.; Espiritu, E.; Toney, M.D.
Conversion of aminodeoxychorismate synthase into anthranilate synthase with Janus mutations: mechanism of pyruvate elimination catalyzed by chorismate enzymes
Biochemistry
54
2372-2384
2015
Escherichia coli (P00903), Escherichia coli
EXTERNAL LINKS (specific for EC-Number 2.6.1.85)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
