Literature summary for 3.1.3.3 extracted from

Chiba, Y.; Horita, S.; Ohtsuka, J.; Arai, H.; Nagata, K.; Igarashi, Y.; Tanokura, M.; Ishii, M.
Structural units important for activity of a novel-type phosphoserine phosphatase from Hydrogenobacter thermophilus TK-6 revealed by crystal structure analysis (2013), J. Biol. Chem., 288, 11448-11458.

Cloned(Commentary)

Cloned (Comment)	Organism
-	Hydrogenobacter thermophilus

Crystallization (Commentary)

Crystallization (Comment)	Organism
apo-form and in complex with its substrate L-phosphoserine, to 1.5 A and 1.8 A resolution, respectively. In the crystal structure of the enzyme-substrate complex, oxygen atoms of the carboxyl group of L-phosphoserine form hydrogen bonds with main-chain amides of Gln21 and Gly22, and Nepsilon2 of Gln21, and partly form a hydrogen or an ionic bond withNepsilon2 of His85. The nitrogen atom of amino group of L-phosphoserine forms a hydrogen or an ionic bond with oxygen atoms of the side-chain carboxyl group of Glu82, and forms hydrogen bonds with Nepsilon2 of His85 and Ogamma1 of Thr15	Hydrogenobacter thermophilus

Crystallization (Comment)

Organism

apo-form and in complex with its substrate L-phosphoserine, to 1.5 A and 1.8 A resolution, respectively. In the crystal structure of the enzyme-substrate complex, oxygen atoms of the carboxyl group of L-phosphoserine form hydrogen bonds with main-chain amides of Gln21 and Gly22, and Nepsilon2 of Gln21, and partly form a hydrogen or an ionic bond withNepsilon2 of His85. The nitrogen atom of amino group of L-phosphoserine forms a hydrogen or an ionic bond with oxygen atoms of the side-chain carboxyl group of Glu82, and forms hydrogen bonds with Nepsilon2 of His85 and Ogamma1 of Thr15

Hydrogenobacter thermophilus

Protein Variants

Protein Variants	Comment	Organism
delI211	50fold decrease in catalytic efficiency	Hydrogenobacter thermophilus
delVal2-I211	400fold decrease in catalytic efficiency	Hydrogenobacter thermophilus
H85A	almost complete loss of activity	Hydrogenobacter thermophilus
H9A	almost complete loss of activity	Hydrogenobacter thermophilus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
1.5	-	L-phosphoserine	pH 8.0, 22°C, wild-type	Hydrogenobacter thermophilus
3.3	-	L-phosphoserine	pH 8.0, 22°C, mutant delI211	Hydrogenobacter thermophilus
15.2	-	L-phosphoserine	pH 8.0, 22°C, mutant delVal2-I211	Hydrogenobacter thermophilus
20	-	L-phosphoserine	above 20 mM, pH 8.0, 22°C, mutant H85A	Hydrogenobacter thermophilus

Organism

Organism	UniProt	Comment	Textmining
Hydrogenobacter thermophilus	D3DFG8	-	-
Hydrogenobacter thermophilus DSM 6534	D3DFG8	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-phosphoserine + H2O	-	Hydrogenobacter thermophilus	L-serine + phosphate	-	?
L-phosphoserine + H2O	-	Hydrogenobacter thermophilus DSM 6534	L-serine + phosphate	-	?

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism
0.24	-	L-phosphoserine	pH 8.0, 22°C, mutant delVal2-I211	Hydrogenobacter thermophilus
2	-	L-phosphoserine	pH 8.0, 22°C, mutant delI211	Hydrogenobacter thermophilus
98	-	L-phosphoserine	pH 8.0, 22°C, wild-type	Hydrogenobacter thermophilus