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EC Tree
IUBMB Comments This bacterial enzyme is present in pathogenic Salmonella species, uropathogenic and avian pathogenic Escherichia coli strains, and certain Klebsiella strains. Unlike EC 3.1.1.108, ferric enterobactin esterase, which acts only on enterobactin, this enzyme can also act on the C-glucosylated forms known as salmochelins. Unlike EC 3.1.1.109, ferric salmochelin esterase (IroD), IroE prefers apo siderophores as substrates, and is assumed to act before the siderophores are exported out of the cell. It hydrolyses the trilactone only once, producing linearized trimers.
The expected taxonomic range for this enzyme is: Escherichia coli
Reaction Schemes
+
=
N-(2,3-dihydroxybenzoyl)-L-serine trimer
Synonyms
enterobactin hydrolase,
iroE ,
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enterobactin hydrolase
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enterobactin hydrolase
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iroE
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diglucosyl-enterobactin + H2O = diglucosyl-(2,3-dihydroxybenzoylserine)3
(3)
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-
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enterobactin + H2O = N-(2,3-dihydroxybenzoyl)-L-serine trimer
(1)
-
-
-
monoglucosyl-enterobactin + H2O = monoglucosyl-(2,3-dihydroxybenzoylserine)3
(4)
-
-
-
triglucosyl-enterobactin + H2O = triglucosyl-(2,3-dihydroxybenzoylserine)3
(2)
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-
-
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apo-salmochelin esterase
This bacterial enzyme is present in pathogenic Salmonella species, uropathogenic and avian pathogenic Escherichia coli strains, and certain Klebsiella strains. Unlike EC 3.1.1.108, ferric enterobactin esterase, which acts only on enterobactin, this enzyme can also act on the C-glucosylated forms known as salmochelins. Unlike EC 3.1.1.109, ferric salmochelin esterase (IroD), IroE prefers apo siderophores as substrates, and is assumed to act before the siderophores are exported out of the cell. It hydrolyses the trilactone only once, producing linearized trimers.
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diglucosyl-enterobactin + H2O
diglucosyl-(2,3-dihydroxybenzoylserine)3
enterobactin + H2O
N-(2,3-dihydroxybenzoyl)-L-serine trimer
ferric diglucosyl-enterobactin + H2O
ferric diglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
ferric enterobactin + H2O
ferric N-(2,3-dihydroxybenzoyl)-L-serine trimer
-
-
-
?
ferric monoglucosyl-enterobactin + H2O
ferric monoglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
ferric triglucosyl-enterobactin + H2O
triglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
monoglucosyl-enterobactin + H2O
monoglucosyl-(2,3-dihydroxybenzoylserine)3
salmochelin S4 + H2O
salmochelin S2
triglucosyl-enterobactin + H2O
triglucosyl-(2,3-dihydroxybenzoylserine)3
additional information
?
-
diglucosyl-enterobactin + H2O
diglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
diglucosyl-enterobactin + H2O
diglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
enterobactin + H2O
N-(2,3-dihydroxybenzoyl)-L-serine trimer
-
-
-
?
enterobactin + H2O
N-(2,3-dihydroxybenzoyl)-L-serine trimer
the enzyme prefers apo siderophores as substrates, and tends to hydrolyze the trilactone just once to produce linearized trimers
-
-
?
enterobactin + H2O
N-(2,3-dihydroxybenzoyl)-L-serine trimer
-
-
-
?
enterobactin + H2O
N-(2,3-dihydroxybenzoyl)-L-serine trimer
the enzyme prefers apo siderophores as substrates, and tends to hydrolyze the trilactone just once to produce linearized trimers
-
-
?
monoglucosyl-enterobactin + H2O
monoglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
monoglucosyl-enterobactin + H2O
monoglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
salmochelin S4 + H2O
salmochelin S2
-
-
-
?
salmochelin S4 + H2O
salmochelin S2
-
-
-
?
triglucosyl-enterobactin + H2O
triglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
triglucosyl-enterobactin + H2O
triglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
additional information
?
-
the enzyme hydrolyzes the Fe3+-bound siderophores very inefficiently. The enzyme hydrolyzes apo forms of siderophores more efficiently than Fe3+-bound ones
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?
additional information
?
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the enzyme hydrolyzes the Fe3+-bound siderophores very inefficiently. The enzyme hydrolyzes apo forms of siderophores more efficiently than Fe3+-bound ones
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?
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diglucosyl-enterobactin + H2O
diglucosyl-(2,3-dihydroxybenzoylserine)3
enterobactin + H2O
N-(2,3-dihydroxybenzoyl)-L-serine trimer
monoglucosyl-enterobactin + H2O
monoglucosyl-(2,3-dihydroxybenzoylserine)3
salmochelin S4 + H2O
salmochelin S2
triglucosyl-enterobactin + H2O
triglucosyl-(2,3-dihydroxybenzoylserine)3
diglucosyl-enterobactin + H2O
diglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
diglucosyl-enterobactin + H2O
diglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
enterobactin + H2O
N-(2,3-dihydroxybenzoyl)-L-serine trimer
-
-
-
?
enterobactin + H2O
N-(2,3-dihydroxybenzoyl)-L-serine trimer
-
-
-
?
monoglucosyl-enterobactin + H2O
monoglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
monoglucosyl-enterobactin + H2O
monoglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
salmochelin S4 + H2O
salmochelin S2
-
-
-
?
salmochelin S4 + H2O
salmochelin S2
-
-
-
?
triglucosyl-enterobactin + H2O
triglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
triglucosyl-enterobactin + H2O
triglucosyl-(2,3-dihydroxybenzoylserine)3
-
-
-
?
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diisopropyl fluorophosphonate
-
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0.039
diglucosyl-enterobactin
at pH 7.5 and 23°C
0.016
enterobactin
at pH 7.5 and 23°C
0.0046
ferric diglucosyl-enterobactin
at pH 7.5 and 23°C
0.0034
ferric enterobactin
at pH 7.5 and 23°C
0.0048
ferric monoglucosyl-enterobactin
at pH 7.5 and 23°C
0.016
ferric triglucosyl-enterobactin
Km above 0.016 mM, at pH 7.5 and 23°C
0.029
monoglucosyl-enterobactin
at pH 7.5 and 23°C
0.155
triglucosyl-enterobactin
at pH 7.5 and 23°C
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5.33
diglucosyl-enterobactin
at pH 7.5 and 23°C
6.25
enterobactin
at pH 7.5 and 23°C
0.04
ferric diglucosyl-enterobactin
at pH 7.5 and 23°C
0.05
ferric enterobactin
at pH 7.5 and 23°C
0.05
ferric monoglucosyl-enterobactin
at pH 7.5 and 23°C
0.13
ferric triglucosyl-enterobactin
turnover number above 0.13 1/sec, at pH 7.5 and 23°C
7.17
monoglucosyl-enterobactin
at pH 7.5 and 23°C
7.5
triglucosyl-enterobactin
at pH 7.5 and 23°C
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133
diglucosyl-enterobactin
at pH 7.5 and 23°C
383
enterobactin
at pH 7.5 and 23°C
8.3
ferric diglucosyl-enterobactin
at pH 7.5 and 23°C
15
ferric enterobactin
at pH 7.5 and 23°C
11.7
ferric monoglucosyl-enterobactin
at pH 7.5 and 23°C
8.3
ferric triglucosyl-enterobactin
at pH 7.5 and 23°C
233
monoglucosyl-enterobactin
at pH 7.5 and 23°C
50
triglucosyl-enterobactin
at pH 7.5 and 23°C
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UniProt
brenda
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UniProt
brenda
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brenda
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brenda
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IROE_ECOL6
Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC)
318
1
35444
Swiss-Prot
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?
x * 35000, SDS-PAGE
?
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x * 35000, SDS-PAGE
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monomer
1 * 30800, calculated from amino acid sequence
monomer
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1 * 30800, calculated from amino acid sequence
-
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native enzyme and enzyme in complex with diisopropyl fluorophosphonate, sitting drop vapor diffusion method, using 6-10% (w/v) PEG 3350 and 100 mM HEPES (pH 7.5)
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E253Q
the mutant shows 92% activity with enterobactin and 97% activity with diglucosyl-enterobactin compared to the wild type enzyme
S245E
the mutant shows 84% activity with enterobactin and 66% activity with diglucosyl-enterobactin compared to the wild type enzyme
S245D
the mutant shows 60% activity with enterobactin and 60% activity with diglucosyl-enterobactin compared to the wild type enzyme
R130K
the mutant shows 0.036% activity with enterobactin and 0.41% activity with diglucosyl-enterobactin compared to the wild type enzyme
D250A
the mutant shows 59% activity with enterobactin and 72% activity with diglucosyl-enterobactin compared to the wild type enzyme
E253A
the mutant shows 78% activity with enterobactin and 86% activity with diglucosyl-enterobactin compared to the wild type enzyme
D90N
the mutant shows 1.5% activity with enterobactin and 1.5% activity with diglucosyl-enterobactin compared to the wild type enzyme
D90A
the mutant shows 0.4% activity with enterobactin and 0.56% activity with diglucosyl-enterobactin compared to the wild type enzyme
D250N
the mutant shows 72% activity with enterobactin and 62% activity with diglucosyl-enterobactin compared to the wild type enzyme
D90N
-
the mutant shows 1.5% activity with enterobactin and 1.5% activity with diglucosyl-enterobactin compared to the wild type enzyme
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D90A
-
the mutant shows 0.4% activity with enterobactin and 0.56% activity with diglucosyl-enterobactin compared to the wild type enzyme
-
D250A
-
the mutant shows 59% activity with enterobactin and 72% activity with diglucosyl-enterobactin compared to the wild type enzyme
-
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Ni-NTA column chromatography
Ni-NTA column chromatography and Superdex S200 gel filtration
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expressed in Escherichia coli BL21(DE3) cells
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Larsen, N.; Lin, H.; Wei, R.; Fischbach, M.; Walsh, C.
Structural characterization of enterobactin hydrolase IroE
Biochemistry
45
10184-10190
2006
Escherichia coli (A0A0H2V871), Escherichia coli CFT073 (A0A0H2V871), Escherichia coli CFT073
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Lin, H.; Fischbach, M.; Liu, D.; Walsh, C.
In vitro characterization of salmochelin and enterobactin trilactone hydrolases IroD, IroE, and Fes
J. Am. Chem. Soc.
127
11075-11084
2005
Escherichia coli (A0A0H2V871), Escherichia coli CFT073 (A0A0H2V871)
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History
Enzyme Nomenclature
3.1.1.107 apo-salmochelin esterase
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