Results 151 to 160 of about 465,841 (199)

Structural and Enzymological Characterization of Phosphoserine Phosphatase From Brucella melitensis

Proteins: Structure, Function, and Bioinformatics
Amino acid L‐serine (L‐Ser) is a precursor of various biomolecules, including other amino acids, glutathione, and nucleotides. The metabolism of this amino acid is crucial in diseases such as brucellosis.
Tanguy Scaillet, E. Pierson, Marianne Fillet, Johan Wouters   +3 more
semanticscholar   +4 more sources

High-resolution structure of human phosphoserine phosphatase in open conformation

Acta Crystallographica Section D: Biological Crystallography, 2003
The crystal structure of human phosphoserine phosphatase (HPSP) in the open conformation has been determined at a resolution of 1.53 A. The crystals are orthorhombic, belonging to space group C222(1), with unit-cell parameters a = 49.03, b = 130.25, c = 157.29 A. The asymmetric unit contains two molecules.
Jean-François Collet, Emile Van Schaftingen, Anja Rabijns   +2 more
exaly   +4 more sources

Some of the next articles are maybe not open access.

Related searches:

Molecular survey of the phosphoserine phosphatase involved in L-serine synthesis by silkworms (Bombyx mori)

Insect Molecular Biology, 2020
Phosphoserine phosphatase (PSP) catalyses the synthesis of l‐serine via the phosphorylated pathway by facilitating the dephosphorylation of phosphoserine.
Shigeki Furuya
exaly   +2 more sources

Human phosphoserine phosphatase with serine and phosphate

, 2019
The equilibrium between phosphorylation and dephosphorylation is one of the most important processes that takes place in living cells. Human phosphoserine phosphatase (hPSP) is a key enzyme in the production of serine by the dephosphorylation of phospho ...
J. Wouters, M. Haufroid, M. Mirgaux
semanticscholar   +4 more sources

Novel phosphoserine phosphatase inhibitors

European Journal of Pharmacology, 1997
Phosphoserine phosphatase (EC 3.1.1.3) catalyzes the final step in the major pathway of L-serine biosynthesis in brain. This enzyme may also regulate the levels of glycine and D-serine, the known and putative co-agonists for the glycine site of the N-methyl-D-aspartate receptor in caudal and rostral brain regions, respectively. Using L-phosphoserine as
Paul L Wood, Jon E Hawkinson
exaly   +3 more sources

Human phosphoserine phosphatase with substrate analogue homo-cysteic acid

, 2019
The equilibrium between phosphorylation and dephosphorylation is one of the most important processes that takes place in living cells. Human phosphoserine phosphatase (hPSP) is a key enzyme in the production of serine by the dephosphorylation of phospho ...
J. Wouters, M. Haufroid, M. Mirgaux
semanticscholar   +2 more sources

Characterization of a Non‐Classic Type Phosphoserine Phosphatase Homolog in Thermodesulfidibacter takaii, a Thermophilic, Autotrophic Bacterium in the Phylum Aquificae

The FASEB Journal, 2021
Phosphoserine phosphatase (PSP) catalyzes the dephosphorylation of phosphoserine to serine, and is found in all three domains of life. Classic, metal‐dependent PSPs (dPSPs) belong to the haloacid dehalogenase‐like hydrolase superfamily.
M. Wintzer, Ryuhei Nakamura, Y. Chiba
semanticscholar   +1 more source

Phosphoserine phosphatase of vertebrates

Comparative Biochemistry and Physiology, 1966
Abstract 1. 1. Phosphatase activity of phosphoserine has been measured in the liver of rat, guinea-pig, rabbit, chicken, duck, pigeon, goose, turtle, frog, tench and eel. 2. 2. The liver of all the animals which we have studied is capable of splitting phosphoserine, but only rat, chicken and turtle liver contains a specific phosphoserine ...
M A, Grillo, M, Coghe
openaire   +2 more sources

Regulatory Mechanism of Mycobacterium tuberculosis Phosphoserine Phosphatase SerB2.

Biochemistry, 2017
Almost all organisms contain the same biosynthetic pathway for the synthesis of l-serine from the glycolytic intermediate, d-3-phosphoglycerate. However, regulation of this pathway varies from organism to organism. Many organisms control the activity of the first enzyme in the pathway, d-3-phosphoglycerate dehydrogenase (PGDH), by feedback inhibition ...
G. Grant
semanticscholar   +3 more sources

Cerebral glycine content and phosphoserine phosphatase activity in hyperaminoacidemias

Neurochemical Research, 1987
Chronic hyperphenylalaninemia maintained with the aid of a suppressor of phenylalanine hydroxylase, alpha-methylphenylalanine, increases the glycine concentration and the phosphoserine phosphatase activity of the developing rat brain but not that of liver or kidney. Similar increases occur after daily injections with large doses of phenylalanine alone,
Olga Greengard, O Greengard
exaly   +3 more sources