Literature summary for 3.4.17.18 extracted from

Akparov, V.K.; Timofeev, V.I.; Khaliullin, I.G.; Konstantinova, G.E.; Kuranova, I.P.; Rakitina, T.V.; Svedas, V.K.
Mobile loop in the active site of metallocarboxypeptidases as an underestimated determinant of substrate specificity (2018), Biochemistry (Moscow), 83, 1594-1602 .

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Cloned(Commentary)

Cloned (Comment)	Organism
expression of mutant enzyme A243G is carried out Escherichia coli BL21(DE3) pLysS cells	Thermoactinomyces vulgaris

Crystallization (Commentary)

Crystallization (Comment)	Organism
crystals of the mutant enzyme A243G complexed with N-sulfamoyl-L-phenylalanine are formed under the microgravity conditions by the method of counterx02diffusion through a gel layer in a capillary. The structure of the complex of the CPT G215S/A251G/T257A/D260G/T262D mutant with the transition state analogue N-sulfamoyl-L-phenylalanine is solved at a resolution of 1.35 A and compared it with the structure of similar complex formed by carboxypeptidase T	Thermoactinomyces vulgaris

Crystallization (Comment)

Organism

crystals of the mutant enzyme A243G complexed with N-sulfamoyl-L-phenylalanine are formed under the microgravity conditions by the method of counterx02diffusion through a gel layer in a capillary. The structure of the complex of the CPT G215S/A251G/T257A/D260G/T262D mutant with the transition state analogue N-sulfamoyl-L-phenylalanine is solved at a resolution of 1.35 A and compared it with the structure of similar complex formed by carboxypeptidase T

Thermoactinomyces vulgaris

Protein Variants

Protein Variants	Comment	Organism
G215S/A251G/T257A/D260G/T262D	mutant enzyme with the primary specificity pocket fully reproducing the one in pancreatic carboxypeptidase B retains the broad, mainly hydrophobic substrate specificity of the wild-type enzyme	Thermoactinomyces vulgaris

Inhibitors

Inhibitors	Comment	Organism	Structure
N-sulfamoyl-L-phenylalanine	-	Thermoactinomyces vulgaris

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.027	-	N-Carbobenzoxy-Ala-Ala-Leu	wild-type enzyme, pH and temperature not specified in the publication	Thermoactinomyces vulgaris

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	zinc-dependent enzyme	Thermoactinomyces vulgaris

Organism

Organism	UniProt	Comment	Textmining
Thermoactinomyces vulgaris	P29068	-	-

Purification (Commentary)

Purification (Comment)	Organism
mutant enzyme A243G	Thermoactinomyces vulgaris

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
N-carbobenzoxy-Ala-Ala-Leu + H2O	-	Thermoactinomyces vulgaris	N-carbobenzoxy-Ala-Ala + Leu	-	?

Temperature Optimum [°C]

Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
25	-	assay at	Thermoactinomyces vulgaris

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
6	-	N-Carbobenzoxy-Ala-Ala-Leu	wild-type enzyme, pH and temperature not specified in the publication	Thermoactinomyces vulgaris

pH Optimum

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
7.5	-	assay at	Thermoactinomyces vulgaris

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.11	-	N-sulfamoyl-L-phenylalanine	mutant enzyme A243G, pH and temperature not specified in the publication	Thermoactinomyces vulgaris