Phosphoserine

From NuGOwiki

(Redirected from HMDB00272)
Jump to: navigation, search

The NuGOwiki Metabolite Database is a joint initiative of NuGO and HMDB

Taxonomy Navigation Box; search by

All Metabolites | Biochemical | Nutritional | Functional | Metabolic Pathways | Diseases | Phenotypes | Physiological Processes | Protein

Phosphoserine
2D structure for Phosphoserine
Chemical Name (2S)-2-amino-3-phosphonooxy-propanoic acid
Chemical Formula C3H8NO6P
CAS Number 407-41-0
Chemical Information HMDB00272
Biochemical Taxonomy

  • Amino Acid Phosphates

Functional Taxonomy Not Available
Nutritional Taxonomy Not Available
Metabolic Pathways

  • Vitamin B6 Metabolism

Biofluid Location

  • Blood
  • Cerebrospinal Fluid (CSF)
  • Urine

Tissue Location Not Available
Normal Biofluid Concentrations

  • Blood: 17.0 +/- 3.0 umol/L
  • Cerebrospinal Fluid (CSF): 4.2 +/- 1.7 uM
  • Cerebrospinal Fluid (CSF): 5.0 +/- 0.9 uM
  • Urine: 4.605 (1.645-7.566) umol/mmol creatinine

Normal Tissue Concentrations Not Available
Diseases / Conditions Related to Nutrition Not Available
Other (Monogenic Disorders) Not Available
Abnormal Biofluid Concentrations Not Available
Abnormal Tissue Concentrations Not Available
Physiological Processes Not Available
Authors:
Affiliations:

Contents

Introduction

guidelines
The phosphoric acid ester of serine. As a constituent (residue) of proteins, its side chain can undergo O-linked glycosylation. This might be important in explaining some of the devastating consequences of diabetes. It is one of three amino acid residues that are commonly phosphorylated by kinases during cell signalling in eukaryotes. Phosphorylated serine residues are often referred to as phosphoserine. Serine proteases are a common type of protease. Serine, organic compound, one of the 20 amino acids commonly found in animal proteins. Only the L-stereoisomer appears in mammalian protein. It is not essential to the human diet, since it can be synthesized in the body from other metabolites, including glycine. Serine was first obtained from silk protein, a particularly rich source, in 1865. Its name is derived from the Latin for silk, sericum. Serine's structure was established in 1902.

Biological Function

guidelines

Catabolism

guidelines

Diseases / Conditions Related to Nutrition

guidelines


Other (Monogenic) Disorders

guidelines


Nutritional Information

guidelines

Drivers for biological variation

guidelines

Vulnerable groups

guidelines

Other resources

guidelines

Links

guidelines