Literature summary for 3.5.3.6 extracted from

Li, L.; Li, Z.; Chen, D.; Lu, X.; Feng, X.; Wright, E.C.; Solberg, N.O.; Dunaway-Mariano, D.; Mariano, P.S.; Galkin, A.; Kulakova, L.; Herzberg, O.; Green-Church, K.B.; Zhang, L.
Inactivation of microbial arginine deiminases by L-canavanine (2008), J. Am. Chem. Soc., 130, 1918-1931.

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Crystallization (Commentary)

Crystallization (Comment)	Organism
X-ray crystallographic coordinates for the structure of the C406A ADI -L-arginine complex, overview	Pseudomonas aeruginosa

Inhibitors

Inhibitors	Comment	Organism	Structure
L-canavanine	two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview	Bacillus cereus
L-canavanine	two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview	Burkholderia mallei
L-canavanine	two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview	Escherichia coli
L-canavanine	two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview	Giardia intestinalis
L-canavanine	competitive; two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview	Pseudomonas aeruginosa

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.09	-	L-arginine	pH 7.0, 25°C	Bacillus cereus
0.09	-	L-arginine	pH 5.6, 25°C	Burkholderia mallei
0.14	-	L-arginine	pH 5.6, 25°C	Pseudomonas aeruginosa
0.16	-	L-arginine	pH 7.5, 25°C	Giardia intestinalis
0.32	-	L-arginine	pH 6.0, 25°C	Escherichia coli
0.7	-	L-canavanine	pH 5.6, 25°C	Pseudomonas aeruginosa
1.2	-	L-canavanine	pH 5.6, 25°C	Burkholderia mallei
1.9	-	L-canavanine	pH 7.5, 25°C	Giardia intestinalis
2.1	-	L-canavanine	pH 6.0, 25°C	Escherichia coli
2.3	-	L-canavanine	pH 7.0, 25°C	Bacillus cereus

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	-	Escherichia coli
Mg2+	-	Pseudomonas aeruginosa

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
L-arginine + H2O	Escherichia coli	-	L-citrulline + NH3	-	?
L-arginine + H2O	Giardia intestinalis	-	L-citrulline + NH3	-	?
L-arginine + H2O	Pseudomonas aeruginosa	-	L-citrulline + NH3	-	?
L-arginine + H2O	Bacillus cereus	-	L-citrulline + NH3	-	?
L-arginine + H2O	Burkholderia mallei	-	L-citrulline + NH3	-	?

Organism

Organism	UniProt	Comment	Textmining
Bacillus cereus	-	-	-
Burkholderia mallei	-	-	-
Escherichia coli	-	-	-
Giardia intestinalis	-	-	-
Pseudomonas aeruginosa	-	-	-
Pseudomonas aeruginosa	P13981	-	-

Reaction

Reaction	Comment	Organism	Reaction ID
L-arginine + H2O = L-citrulline + NH3	the chemical mechanism for ADI catalysis involves initial formation and subsequent hydrolysis of a Cys-alkylthiouronium ion intermediate	Escherichia coli	a
L-arginine + H2O = L-citrulline + NH3	the chemical mechanism for ADI catalysis involves initial formation and subsequent hydrolysis of a Cys-alkylthiouronium ion intermediate	Giardia intestinalis	a
L-arginine + H2O = L-citrulline + NH3	the chemical mechanism for ADI catalysis involves initial formation and subsequent hydrolysis of a Cys-alkylthiouronium ion intermediate	Pseudomonas aeruginosa	a
L-arginine + H2O = L-citrulline + NH3	the chemical mechanism for ADI catalysis involves initial formation and subsequent hydrolysis of a Cys-alkylthiouronium ion intermediate	Bacillus cereus	a
L-arginine + H2O = L-citrulline + NH3	the chemical mechanism for ADI catalysis involves initial formation and subsequent hydrolysis of a Cys-alkylthiouronium ion intermediate	Burkholderia mallei	a
L-arginine + H2O = L-citrulline + NH3	chemical mechanism for ADI catalysis involves initial formation and subsequent hydrolysis of a Cys-alkylthiouronium ion intermediate, PaADI employs an active site Cys in nucleophilic catalysis	Pseudomonas aeruginosa	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-arginine + H2O	-	Escherichia coli	L-citrulline + NH3	-	?
L-arginine + H2O	-	Giardia intestinalis	L-citrulline + NH3	-	?
L-arginine + H2O	-	Pseudomonas aeruginosa	L-citrulline + NH3	-	?
L-arginine + H2O	-	Bacillus cereus	L-citrulline + NH3	-	?
L-arginine + H2O	-	Burkholderia mallei	L-citrulline + NH3	-	?
L-canavanine + H2O	two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview	Escherichia coli	O-ureido-L-homoserine + NH3	-	?
L-canavanine + H2O	two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview	Giardia intestinalis	O-ureido-L-homoserine + NH3	-	?
L-canavanine + H2O	two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview	Pseudomonas aeruginosa	O-ureido-L-homoserine + NH3	-	?
L-canavanine + H2O	two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview	Bacillus cereus	O-ureido-L-homoserine + NH3	-	?
L-canavanine + H2O	two competing pathways, slow substrate inhibition or irreversible inhibition, branch at the Cys-alkylthiouronium ion intermediate: one pathway leads to direct formation of O-ureido-L-homoserine via a reactive thiouronium intermediate. The other pathway leads to an inactive form of the enzyme, a Cys-alkylisothiourea adduct, mechanism and structure, overview	Burkholderia mallei	O-ureido-L-homoserine + NH3	-	?
L-canavanine + H2O	slow substrate, reaction via Cys-alkylthiouronium ion intermediate, two competing pathways follow that branch at the Cys-alkylthiouronium ion intermediate, overview	Pseudomonas aeruginosa	O-ureido-L-homoserine + NH3	-	?

Subunits

Subunits	Comment	Organism
More	structure of the ADI-L-arginine complex, overview	Pseudomonas aeruginosa

Synonyms

Synonyms	Comment	Organism
ADI	-	Escherichia coli
ADI	-	Giardia intestinalis
ADI	-	Pseudomonas aeruginosa
ADI	-	Bacillus cereus
ADI	-	Burkholderia mallei

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Escherichia coli
25	-	assay at	Giardia intestinalis
25	-	assay at	Pseudomonas aeruginosa
25	-	assay at	Bacillus cereus
25	-	assay at	Burkholderia mallei

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.09	-	L-canavanine	pH 5.6, 25°C	Burkholderia mallei
0.32	-	L-canavanine	pH 7.5, 25°C	Giardia intestinalis
0.42	-	L-canavanine	pH 6.0, 25°C	Escherichia coli
0.46	-	L-canavanine	pH 7.0, 25°C	Bacillus cereus
0.62	-	L-canavanine	pH 5.6, 25°C	Pseudomonas aeruginosa
1.3	-	L-arginine	pH 5.6, 25°C	Burkholderia mallei
2.6	-	L-arginine	pH 7.5, 25°C	Giardia intestinalis
3.2	-	L-arginine	pH 6.0, 25°C	Escherichia coli
4.4	-	L-arginine	pH 7.0, 25°C	Bacillus cereus
6.3	-	L-arginine	pH 5.6, 25°C	Pseudomonas aeruginosa

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
5.6	-	-	Pseudomonas aeruginosa
5.6	-	-	Burkholderia mallei
5.6	-	assay at	Pseudomonas aeruginosa
6	-	-	Escherichia coli
7	-	-	Bacillus cereus
7.5	-	-	Giardia intestinalis

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
1.7	-	L-canavanine	pH 5.6, 25°C	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)