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Record Information
Version3.6
Creation Date2005-11-16 15:48:42 UTC
Update Date2014-06-11 21:20:40 UTC
HMDB IDHMDB00187
Secondary Accession Numbers
  • HMDB00589
Metabolite Identification
Common NameL-Serine
DescriptionSerine is a nonessential amino acid derived from glycine. Like all the amino acid building blocks of protein and peptides, serine can become essential under certain conditions, and is thus important in maintaining health and preventing disease. Low-average concentration of serine compared to other amino acids is found in muscle. Serine is highly concentrated in all cell membranes. (http://www.dcnutrition.com/AminoAcids/) L-Serine may be derived from four possible sources: dietary intake; biosynthesis from the glycolytic intermediate 3-phosphoglycerate; from glycine ; and by protein and phospholipid degradation. Little data is available on the relative contributions of each of these four sources of l-serine to serine homoeostasis. It is very likely that the predominant source of l-serine will be very different in different tissues and during different stages of human development. In the biosynthetic pathway, the glycolytic intermediate 3-phosphoglycerate is converted into phosphohydroxypyruvate, in a reaction catalyzed by 3-phosphoglycerate dehydrogenase (3- PGDH; EC 1.1.1.95). Phosphohydroxypyruvate is metabolized to phosphoserine by phosphohydroxypyruvate aminotransferase (EC 2.6.1.52) and, finally, phosphoserine is converted into l-serine by phosphoserine phosphatase (PSP; EC 3.1.3.3). In liver tissue, the serine biosynthetic pathway is regulated in response to dietary and hormonal changes. Of the three synthetic enzymes, the properties of 3-PGDH and PSP are the best documented. Hormonal factors such as glucagon and corticosteroids also influence 3-PGDH and PSP activities in interactions dependent upon the diet. L-serine plays a central role in cellular proliferation. L-Serine is the predominant source of one-carbon groups for the de novo synthesis of purine nucleotides and deoxythymidine monophosphate. It has long been recognized that, in cell cultures, L-serine is a conditional essential amino acid, because it cannot be synthesized in sufficient quantities to meet the cellular demands for its utilization. In recent years, L-serine and the products of its metabolism have been recognized not only to be essential for cell proliferation, but also to be necessary for specific functions in the central nervous system. The findings of altered levels of serine and glycine in patients with psychiatric disorders and the severe neurological abnormalities in patients with defects of L-serine synthesis underscore the importance of L-serine in brain development and function. (PMID 12534373 ).
Structure
Thumb
Synonyms
  1. (-)-Serine
  2. (S)-2-amino-3-hydroxy-Propanoate
  3. (S)-2-amino-3-hydroxy-Propanoic acid
  4. (S)-2-Amino-3-hydroxypropanoate
  5. (S)-2-Amino-3-hydroxypropanoic acid
  6. (S)-a-Amino-b-hydroxypropionate
  7. (S)-a-Amino-b-hydroxypropionic acid
  8. (S)-alpha-Amino-beta-hydroxypropionate
  9. (S)-alpha-Amino-beta-hydroxypropionic acid
  10. (S)-b-Amino-3-hydroxypropionate
  11. (S)-b-Amino-3-hydroxypropionic acid
  12. (S)-beta-Amino-3-hydroxypropionate
  13. (S)-beta-Amino-3-hydroxypropionic acid
  14. (S)-Serine
  15. 2-Amino-3-hydroxypropanoate
  16. 2-Amino-3-hydroxypropanoic acid
  17. 3-Hydroxy-L-Alanine
  18. b-Hydroxy-L-alanine
  19. beta-Hydroxy-L-alanine
  20. beta-Hydroxyalanine
  21. L-(-)-Serine
  22. L-3-Hydroxy-2-aminopropionate
  23. L-3-Hydroxy-2-aminopropionic acid
  24. L-3-Hydroxy-alanine
  25. L-Ser
  26. Serine
Chemical FormulaC3H7NO3
Average Molecular Weight105.0926
Monoisotopic Molecular Weight105.042593095
IUPAC Name(2S)-2-amino-3-hydroxypropanoic acid
Traditional IUPAC NameL-serine
CAS Registry Number56-45-1
SMILES
N[C@@H](CO)C(O)=O
InChI Identifier
InChI=1S/C3H7NO3/c4-2(1-5)3(6)7/h2,5H,1,4H2,(H,6,7)/t2-/m0/s1
InChI KeyMTCFGRXMJLQNBG-REOHCLBHSA-N
Chemical Taxonomy
KingdomOrganic Compounds
Super ClassAmino Acids, Peptides, and Analogues
ClassAmino Acids and Derivatives
Sub ClassAlpha Amino Acids and Derivatives
Other Descriptors
  • Aliphatic Acyclic Compounds
  • Amino fatty acids(Lipidmaps)
  • amino acid zwitterion(ChEBI)
Substituents
  • 1,2 Aminoalcohol
  • Beta Hydroxy Acid
  • Carboxylic Acid
  • Primary Alcohol
  • Primary Aliphatic Amine (Alkylamine)
Direct ParentAlpha Amino Acids and Derivatives
Ontology
StatusDetected and Quantified
Origin
  • Endogenous
Biofunction
  • Component of Aminoacyl-tRNA biosynthesis
  • Component of Cyanoamino acid metabolism
  • Component of Cysteine metabolism
  • Component of Glycine, serine and threonine metabolism
  • Component of Glycosphingolipid metabolism
  • Component of Methane metabolism
  • Component of Methionine metabolism
  • Component of Selenoamino acid metabolism
ApplicationNot Available
Cellular locations
  • Cytoplasm
  • Extracellular
  • Mitochondria
  • Peroxisome
Physical Properties
StateSolid
Experimental Properties
PropertyValueReference
Melting Point228 °CNot Available
Boiling PointNot AvailableNot Available
Water Solubility425.0 mg/mLNot Available
LogP-3.07HANSCH,C ET AL. (1995)
Predicted Properties
PropertyValueSource
water solubility480 g/LALOGPS
logP-3.4ALOGPS
logP-3.9ChemAxon
logS0.66ALOGPS
pKa (strongest acidic)2.03ChemAxon
pKa (strongest basic)8.93ChemAxon
physiological charge0ChemAxon
hydrogen acceptor count4ChemAxon
hydrogen donor count3ChemAxon
polar surface area83.55ChemAxon
rotatable bond count2ChemAxon
refractivity22.04ChemAxon
polarizability9.45ChemAxon
Spectra
SpectraGC-MSMS/MSLC-MS1D NMR2D NMR
Biological Properties
Cellular Locations
  • Cytoplasm
  • Extracellular
  • Mitochondria
  • Peroxisome
Biofluid Locations
  • Blood
  • Cerebrospinal Fluid (CSF)
  • Urine
Tissue Location
  • All Tissues
  • Prostate
Pathways
NameSMPDB LinkKEGG Link
Ammonia RecyclingSMP00009map00910
Glycine and Serine MetabolismSMP00004map00260
Homocysteine DegradationSMP00455Not Available
Methionine MetabolismSMP00033map00270
Sphingolipid MetabolismSMP00034map00500
Normal Concentrations
BiofluidStatusValueAgeSexConditionReferenceDetails
BloodDetected and Quantified159.8 +/- 26.6 uMAdult (>18 years old)Not SpecifiedNormal details
BloodDetected and Quantified173.2 +/- 51.3 uMAdult (>18 years old)Not SpecifiedNormal details
BloodDetected and Quantified114.0 (95.0-133.0) uMAdult (>18 years old)BothNormal details
BloodDetected and Quantified134.0 +/- 38.0 uMNewborn (0-30 days old)Not SpecifiedNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified121.0 +/- 25.0 uMChildren (1-13 years old)MaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified127.0 +/- 27.0 uMChildren (1-13 years old)FemaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified114.0 +/- 23.0 uMAdult (>18 years old)MaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified127.0 +/- 29.0 uMAdult (>18 years old)FemaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified121.0 +/- 14.0 uMChildren (1-13 years old)Not SpecifiedNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified137.0 +/- 35.0 uMAdult (>18 years old)MaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified142.0 +/- 35.0 uMAdult (>18 years old)FemaleNormal
    • Geigy Scientific ...
details
BloodDetected and Quantified70.3 +/- 19.6 uMAdult (>18 years old)MaleNormal details
BloodDetected and Quantified236.0 +/- 6.0 uMAdult (>18 years old)BothNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified28.9 (20.7-37.0) uMAdult (>18 years old)BothNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified24.5 +/- 4.4 uMAdult (>18 years old)BothNormal
    • Geigy Scientific ...
details
Cerebrospinal Fluid (CSF)Detected and Quantified42 +/- 18 uMNot SpecifiedBothNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified42.4 +/- 15.1 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified28.1 +/- 4.7 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified30.2 +/- 3.8 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified32.8 +/- 8.6 uMAdult (>18 years old)Not SpecifiedNormal details
Cerebrospinal Fluid (CSF)Detected and Quantified7.6 +/- 0.67 uMAdult (>18 years old)BothNormal details
UrineDetected and Quantified19.0 (10.4-35.8) umol/mmol creatinineAdult (>18 years old)Both
Normal
details
UrineDetected and Quantified33.6 umol/mmol creatinineAdult (>18 years old)BothNormal details
UrineDetected and Quantified19.04-47.60 umol/mmol creatinineAdult (>18 years old)BothNormal
    • David F. Putnam C...
details
UrineDetected and Quantified25.3 (11.6-53.4) umol/mmol creatinineAdult (>18 years old)Both
Normal
details
UrineDetected and Quantified33.83 umol/mmol creatinineAdult (>18 years old)MaleNormal
    • Shaykhutdinov RA,...
details
UrineDetected and Quantified27.38 +/- 9.54 umol/mmol creatinineAdult (>18 years old)BothNormal details
UrineDetected and Quantified24.5 (12.3-50.2) umol/mmol creatinineAdult (>18 years old)Both
Normal
details
UrineDetected and Quantified2.6 (0.37-5.0) umol/mmol creatinineNewborn (0-30 days old)BothNormal
    • Geigy Scientific ...
    • West Cadwell, N.J...
    • Basel, Switzerlan...
details
UrineDetected and Quantified8.9 +/- 4.6 umol/mmol creatinineChildren (1-13 years old)FemaleNormal
    • Geigy Scientific ...
    • West Cadwell, N.J...
    • Basel, Switzerlan...
details
UrineDetected and Quantified30.0 +/- 13.6 umol/mmol creatinineAdult (>18 years old)MaleNormal
    • Geigy Scientific ...
    • West Cadwell, N.J...
    • Basel, Switzerlan...
details
UrineDetected and Quantified26.0 +/- 10.0 umol/mmol creatinineAdult (>18 years old)FemaleNormal
    • Geigy Scientific ...
    • West Cadwell, N.J...
    • Basel, Switzerlan...
details
UrineDetected and Quantified28.5 (12.5-44.4) umol/mmol creatinineAdult (>18 years old)BothNormal
    details
    UrineDetected and Quantified74.67 +/- 37.74 umol/mmol creatinineInfant (0-1 year old)BothNormal details
    UrineDetected and Quantified31.6 umol/mmol creatinineAdult (>18 years old)BothNormal details
    Abnormal Concentrations
    BiofluidStatusValueAgeSexConditionReferenceDetails
    BloodDetected and Quantified104.0 (101.0-107.0) uMAdult (>18 years old)BothRefractory localization-related epilepsy (RLE) details
    BloodDetected and Quantified140.0 (131.0-148.0) uMChildren (1-13 years old)BothJuvenile myoclonic epilepsy (JME) details
    BloodDetected and Quantified197.9 +/- 46.4 uMAdult (>18 years old)BothSchizophrenia details
    BloodDetected and Quantified0.21 +/- 0.024 uMElderly (>65 years old)BothAlzheimer's disease details
    BloodDetected and Quantified221.0 +/- 8.0 uMAdult (>18 years old)Both
    Heart failure
    details
    Cerebrospinal Fluid (CSF)Detected and Quantified38.3 +/- 15.5 uMChildren (1-13 years old)Not SpecifiedLeukemia details
    Cerebrospinal Fluid (CSF)Detected and Quantified31.9 +/- 8.8 uMChildren (1-13 years old)Not Specified
    Leukemia
    details
    Cerebrospinal Fluid (CSF)Detected and Quantified7.5 +/- 0.87 uMAdult (>18 years old)BothSchizophrenia details
    UrineDetected and Quantified0.0041 - 0.0122 umol/mmol creatinineAdult (>18 years old)BothADPKD details
    Associated Disorders and Diseases
    Disease References
    Alzheimer's disease
    1. Fonteh AN, Harrington RJ, Tsai A, Liao P, Harrington MG: Free amino acid and dipeptide changes in the body fluids from Alzheimer's disease subjects. Amino Acids. 2007 Feb;32(2):213-24. Epub 2006 Oct 10. Pubmed: 17031479
    Schizophrenia
    1. Hashimoto K, Fukushima T, Shimizu E, Komatsu N, Watanabe H, Shinoda N, Nakazato M, Kumakiri C, Okada S, Hasegawa H, Imai K, Iyo M: Decreased serum levels of D-serine in patients with schizophrenia: evidence in support of the N-methyl-D-aspartate receptor hypofunction hypothesis of schizophrenia. Arch Gen Psychiatry. 2003 Jun;60(6):572-6. Pubmed: 12796220
    2. Do KQ, Lauer CJ, Schreiber W, Zollinger M, Gutteck-Amsler U, Cuenod M, Holsboer F: gamma-Glutamylglutamine and taurine concentrations are decreased in the cerebrospinal fluid of drug-naive patients with schizophrenic disorders. J Neurochem. 1995 Dec;65(6):2652-62. Pubmed: 7595563
    Heart failure
    1. Norrelund H, Wiggers H, Halbirk M, Frystyk J, Flyvbjerg A, Botker HE, Schmitz O, Jorgensen JO, Christiansen JS, Moller N: Abnormalities of whole body protein turnover, muscle metabolism and levels of metabolic hormones in patients with chronic heart failure. J Intern Med. 2006 Jul;260(1):11-21. Pubmed: 16789974
    Juvenile myoclonic epilepsy
    1. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. Pubmed: 14992292
    Leukemia
    1. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. Pubmed: 15911239
    Refractory localization-related epilepsy
    1. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. Pubmed: 14992292
    Associated OMIM IDs
    DrugBank IDDB00133
    DrugBank Metabolite IDNot Available
    Phenol Explorer Compound IDNot Available
    Phenol Explorer Metabolite IDNot Available
    FoodDB IDFDB012739
    KNApSAcK IDC00001393
    Chemspider ID5736
    KEGG Compound IDC00065
    BioCyc IDSER
    BiGG ID33717
    Wikipedia LinkL-Serine
    NuGOwiki LinkHMDB00187
    Metagene LinkHMDB00187
    METLIN ID5203
    PubChem Compound5951
    PDB IDSER
    ChEBI ID17115
    References
    Synthesis ReferenceQin, Wei-min; Cao, Fei; Zhou, Hua; Li, Zhen-jiang; Wei, Ping. Asymmetric synthesis of D- and L-serine with "Glycine equivalent" method. Huaxue Shiji (2005), 27(11), 643-644, 670.
    Material Safety Data Sheet (MSDS)Download (PDF)
    General References
    1. Kaumeyer JF, Polazzi JO, Kotick MP: The mRNA for a proteinase inhibitor related to the HI-30 domain of inter-alpha-trypsin inhibitor also encodes alpha-1-microglobulin (protein HC). Nucleic Acids Res. 1986 Oct 24;14(20):7839-50. Pubmed: 2430261
    2. Sreekumar A, Poisson LM, Rajendiran TM, Khan AP, Cao Q, Yu J, Laxman B, Mehra R, Lonigro RJ, Li Y, Nyati MK, Ahsan A, Kalyana-Sundaram S, Han B, Cao X, Byun J, Omenn GS, Ghosh D, Pennathur S, Alexander DC, Berger A, Shuster JR, Wei JT, Varambally S, Beecher C, Chinnaiyan AM: Metabolomic profiles delineate potential role for sarcosine in prostate cancer progression. Nature. 2009 Feb 12;457(7231):910-4. Pubmed: 19212411
    3. Nicholson JK, O'Flynn MP, Sadler PJ, Macleod AF, Juul SM, Sonksen PH: Proton-nuclear-magnetic-resonance studies of serum, plasma and urine from fasting normal and diabetic subjects. Biochem J. 1984 Jan 15;217(2):365-75. Pubmed: 6696735
    4. Engelborghs S, Marescau B, De Deyn PP: Amino acids and biogenic amines in cerebrospinal fluid of patients with Parkinson's disease. Neurochem Res. 2003 Aug;28(8):1145-50. Pubmed: 12834252
    5. Hagenfeldt L, Bjerkenstedt L, Edman G, Sedvall G, Wiesel FA: Amino acids in plasma and CSF and monoamine metabolites in CSF: interrelationship in healthy subjects. J Neurochem. 1984 Mar;42(3):833-7. Pubmed: 6198473
    6. Peng CT, Wu KH, Lan SJ, Tsai JJ, Tsai FJ, Tsai CH: Amino acid concentrations in cerebrospinal fluid in children with acute lymphoblastic leukemia undergoing chemotherapy. Eur J Cancer. 2005 May;41(8):1158-63. Epub 2005 Apr 14. Pubmed: 15911239
    7. Cynober LA: Plasma amino acid levels with a note on membrane transport: characteristics, regulation, and metabolic significance. Nutrition. 2002 Sep;18(9):761-6. Pubmed: 12297216
    8. Rainesalo S, Keranen T, Palmio J, Peltola J, Oja SS, Saransaari P: Plasma and cerebrospinal fluid amino acids in epileptic patients. Neurochem Res. 2004 Jan;29(1):319-24. Pubmed: 14992292
    9. Fontaine M, Porchet N, Largilliere C, Marrakchi S, Lhermitte M, Aubert JP, Degand P: Biochemical contribution to diagnosis and study of a new case of D-glyceric acidemia/aciduria. Clin Chem. 1989 Oct;35(10):2148-51. Pubmed: 2551543
    10. Furuya S, Watanabe M: Novel neuroglial and glioglial relationships mediated by L-serine metabolism. Arch Histol Cytol. 2003 May;66(2):109-21. Pubmed: 12846552
    11. Haas W, Grabe K, Geis C, Pach T, Stoll K, Fuchs M, Haberl B, Loy C: Recognition and invasion of human skin by Schistosoma mansoni cercariae: the key-role of L-arginine. Parasitology. 2002 Feb;124(Pt 2):153-67. Pubmed: 11860033
    12. Hashimoto K, Engberg G, Shimizu E, Nordin C, Lindstrom LH, Iyo M: Reduced D-serine to total serine ratio in the cerebrospinal fluid of drug naive schizophrenic patients. Prog Neuropsychopharmacol Biol Psychiatry. 2005 Jun;29(5):767-9. Pubmed: 15939521
    13. Castedo M, Ferri KF, Blanco J, Roumier T, Larochette N, Barretina J, Amendola A, Nardacci R, Metivier D, Este JA, Piacentini M, Kroemer G: Human immunodeficiency virus 1 envelope glycoprotein complex-induced apoptosis involves mammalian target of rapamycin/FKBP12-rapamycin-associated protein-mediated p53 phosphorylation. J Exp Med. 2001 Oct 15;194(8):1097-110. Pubmed: 11602639
    14. Liu T, Zhu E, Wang L, Okada T, Yamaguchi A, Okada N: Abnormal expression of Rb pathway-related proteins in salivary gland acinic cell carcinoma. Hum Pathol. 2005 Sep;36(9):962-70. Pubmed: 16153458
    15. Franchi-Gazzola R, Gazzola GC, Dall'Asta V, Guidotti GG: The transport of alanine, serine, and cysteine in cultured human fibroblasts. J Biol Chem. 1982 Aug 25;257(16):9582-7. Pubmed: 6809740
    16. Yamamoto T, Nishizaki I, Nukada T, Kamegaya E, Furuya S, Hirabayashi Y, Ikeda K, Hata H, Kobayashi H, Sora I, Yamamoto H: Functional identification of ASCT1 neutral amino acid transporter as the predominant system for the uptake of L-serine in rat neurons in primary culture. Neurosci Res. 2004 May;49(1):101-11. Pubmed: 15099708
    17. Mackie S, Aitken A: Novel brain 14-3-3 interacting proteins involved in neurodegenerative disease. FEBS J. 2005 Aug;272(16):4202-10. Pubmed: 16098201
    18. Kobza K, Camporeale G, Rueckert B, Kueh A, Griffin JB, Sarath G, Zempleni J: K4, K9 and K18 in human histone H3 are targets for biotinylation by biotinidase. FEBS J. 2005 Aug;272(16):4249-59. Pubmed: 16098205
    19. Whittemore AS, Cirillo PM, Feldman D, Cohn BA: Prostate specific antigen levels in young adulthood predict prostate cancer risk: results from a cohort of Black and White Americans. J Urol. 2005 Sep;174(3):872-6; discussion 876. Pubmed: 16093978
    20. Schulz I, Zeitschel U, Rudolph T, Ruiz-Carrillo D, Rahfeld JU, Gerhartz B, Bigl V, Demuth HU, Rossner S: Subcellular localization suggests novel functions for prolyl endopeptidase in protein secretion. J Neurochem. 2005 Aug;94(4):970-9. Pubmed: 16092940
    21. de Koning TJ, Snell K, Duran M, Berger R, Poll-The BT, Surtees R: L-serine in disease and development. Biochem J. 2003 May 1;371(Pt 3):653-61. Pubmed: 12534373

    Enzymes

    General function:
    Involved in nucleotide binding
    Specific function:
    Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec) (By similarity).
    Gene Name:
    SARS2
    Uniprot ID:
    Q9NP81
    Molecular weight:
    58029.805
    Reactions
    Adenosine triphosphate + L-Serine + tRNA(Ser) → Adenosine monophosphate + Pyrophosphate + L-seryl-tRNA(Ser)details
    Adenosine triphosphate + L-Serine + tRNA(Sec) → Adenosine monophosphate + Pyrophosphate + L-seryl-tRNA(Sec)details
    Adenosine triphosphate + L-Serine + tRNA(Ser) → Adenosine monophosphate + Pyrophosphate + L-Seryl-tRNA(Ser)details
    Adenosine triphosphate + L-Serine + tRNA(Sec) → Adenosine monophosphate + Pyrophosphate + L-Seryl-tRNA(Sec)details
    General function:
    Involved in nucleotide binding
    Specific function:
    Catalyzes the attachment of serine to tRNA(Ser). Is also probably able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec).
    Gene Name:
    SARS
    Uniprot ID:
    P49591
    Molecular weight:
    58776.785
    Reactions
    Adenosine triphosphate + L-Serine + tRNA(Ser) → Adenosine monophosphate + Pyrophosphate + L-seryl-tRNA(Ser)details
    Adenosine triphosphate + L-Serine + tRNA(Sec) → Adenosine monophosphate + Pyrophosphate + L-seryl-tRNA(Sec)details
    Adenosine triphosphate + L-Serine + tRNA(Ser) → Adenosine monophosphate + Pyrophosphate + L-Seryl-tRNA(Ser)details
    Adenosine triphosphate + L-Serine + tRNA(Sec) → Adenosine monophosphate + Pyrophosphate + L-Seryl-tRNA(Sec)details
    References
    1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
    2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
    3. Zhang Y, Cui J, Zhang R, Wang Y, Hong M: A novel fibrinolytic serine protease from the polychaete Nereis (Neanthes) virens (Sars): purification and characterization. Biochimie. 2007 Jan;89(1):93-103. Epub 2006 Aug 22. Pubmed: 16950556
    4. Follis KE, York J, Nunberg JH: Serine-scanning mutagenesis studies of the C-terminal heptad repeats in the SARS coronavirus S glycoprotein highlight the important role of the short helical region. Virology. 2005 Oct 10;341(1):122-9. Pubmed: 16081124
    5. McClendon CL, Vaidehi N, Kam VW, Zhang D, Goddard WA 3rd: Fidelity of seryl-tRNA synthetase to binding of natural amino acids from HierDock first principles computations. Protein Eng Des Sel. 2006 May;19(5):195-203. Epub 2006 Mar 3. Pubmed: 16517553
    General function:
    Involved in catalytic activity
    Specific function:
    Not Available
    Gene Name:
    SDS
    Uniprot ID:
    P20132
    Molecular weight:
    34625.105
    Reactions
    L-Serine → Pyruvic acid + Ammoniadetails
    L-Serine → 2-Aminoacrylic acid + Waterdetails
    References
    1. Overington JP, Al-Lazikani B, Hopkins AL: How many drug targets are there? Nat Rev Drug Discov. 2006 Dec;5(12):993-6. Pubmed: 17139284
    2. Imming P, Sinning C, Meyer A: Drugs, their targets and the nature and number of drug targets. Nat Rev Drug Discov. 2006 Oct;5(10):821-34. Pubmed: 17016423
    3. Velayudhan J, Jones MA, Barrow PA, Kelly DJ: L-serine catabolism via an oxygen-labile L-serine dehydratase is essential for colonization of the avian gut by Campylobacter jejuni. Infect Immun. 2004 Jan;72(1):260-8. Pubmed: 14688104
    4. Snell K, Walker DG: Regulation of hepatic L-serine dehydratase and L-serine-pyruvate aminotransferase in the developing neonatal rat. Biochem J. 1974 Dec;144(3):519-31. Pubmed: 4377655
    5. Wong HC, Lessie TG: Hydroxy amino acid metabolism in Pseudomonas cepacia: role of L-serine deaminase in dissimilation of serine, glycine, and threonine. J Bacteriol. 1979 Oct;140(1):240-5. Pubmed: 500557
    General function:
    Involved in cysteine biosynthetic process from serine
    Specific function:
    Only known pyridoxal phosphate-dependent enzyme that contains heme. Important regulator of hydrogen sulfide, especially in the brain, utilizing cysteine instead of serine to catalyze the formation of hydrogen sulfide. Hydrogen sulfide is a gastratransmitter with signaling and cytoprotective effects such as acting as a neuromodulator in the brain to protect neurons against hypoxic injury (By similarity).
    Gene Name:
    CBS
    Uniprot ID:
    P35520
    Molecular weight:
    60586.05
    Reactions
    L-Serine + Homocysteine → L-Cystathionine + Waterdetails
    L-Serine + Hydrogen sulfide → L-Cysteine + Waterdetails
    L-Serine + Selenohomocysteine → Selenocystathionine + Waterdetails
    References
    1. Sen S, Banerjee R: A pathogenic linked mutation in the catalytic core of human cystathionine beta-synthase disrupts allosteric regulation and allows kinetic characterization of a full-length dimer. Biochemistry. 2007 Apr 3;46(13):4110-6. Epub 2007 Mar 13. Pubmed: 17352495
    2. Qu K, Lee SW, Bian JS, Low CM, Wong PT: Hydrogen sulfide: neurochemistry and neurobiology. Neurochem Int. 2008 Jan;52(1-2):155-65. Epub 2007 Jun 8. Pubmed: 17629356
    General function:
    Involved in metabolic process
    Specific function:
    Not Available
    Gene Name:
    AGXT
    Uniprot ID:
    P21549
    Molecular weight:
    43009.535
    Reactions
    L-Serine + Pyruvic acid → Hydroxypyruvic acid + L-Alaninedetails
    L-Serine + Glyoxylic acid → Hydroxypyruvic acid + Glycinedetails
    References
    1. Ikushiro H, Islam MM, Tojo H, Hayashi H: Molecular characterization of membrane-associated soluble serine palmitoyltransferases from Sphingobacterium multivorum and Bdellovibrio stolpii. J Bacteriol. 2007 Aug;189(15):5749-61. Epub 2007 Jun 8. Pubmed: 17557831
    2. Cowart LA, Hannun YA: Selective substrate supply in the regulation of yeast de novo sphingolipid synthesis. J Biol Chem. 2007 Apr 20;282(16):12330-40. Epub 2007 Feb 23. Pubmed: 17322298
    3. Son JH, Yoo HH, Kim DH: Activation of de novo synthetic pathway of ceramides is responsible for the initiation of hydrogen peroxide-induced apoptosis in HL-60 cells. J Toxicol Environ Health A. 2007 Aug;70(15-16):1310-8. Pubmed: 17654249
    4. Yard BA, Carter LG, Johnson KA, Overton IM, Dorward M, Liu H, McMahon SA, Oke M, Puech D, Barton GJ, Naismith JH, Campopiano DJ: The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis. J Mol Biol. 2007 Jul 27;370(5):870-86. Epub 2007 May 10. Pubmed: 17559874
    General function:
    Involved in catalytic activity
    Specific function:
    Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Required to prevent uracil accumulation in mtDNA. Interconversion of serine and glycine. Associates with mitochondrial DNA.
    Gene Name:
    SHMT2
    Uniprot ID:
    P34897
    Molecular weight:
    54862.125
    Reactions
    5,10-Methylene-THF + Glycine + Water → Tetrahydrofolic acid + L-Serinedetails
    L-Serine + 5,6,7,8-Tetrahydromethanopterin → 5,10-Methylenetetrahydromethanopterin + Glycine + Waterdetails
    General function:
    Involved in catalytic activity
    Specific function:
    Interconversion of serine and glycine.
    Gene Name:
    SHMT1
    Uniprot ID:
    P34896
    Molecular weight:
    53082.18
    Reactions
    5,10-Methylene-THF + Glycine + Water → Tetrahydrofolic acid + L-Serinedetails
    L-Serine + 5,6,7,8-Tetrahydromethanopterin → 5,10-Methylenetetrahydromethanopterin + Glycine + Waterdetails
    General function:
    Involved in transferase activity, transferring nitrogenous groups
    Specific function:
    Serine palmitoyltransferase (SPT). The heterodimer formed with SPTLC2 or SPTLC3 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, with a slight preference for C14-CoA. The SPTLC1-SPTLC2-SPTSSB complex shows a strong preference for C18-CoA substrate, while the SPTLC1-SPTLC3-SPTSSB isozyme displays an ability to use a broader range of acyl-CoAs, without apparent preference.
    Gene Name:
    SPTLC1
    Uniprot ID:
    O15269
    Molecular weight:
    52743.41
    Reactions
    hexadecanoyl-CoA + L-Serine → Coenzyme A + 3-Dehydrosphinganine + CO(2)details
    hexadecanoyl-CoA + L-Serine → 3-Dehydrosphinganine + Coenzyme A + Carbon dioxidedetails
    References
    1. Yard BA, Carter LG, Johnson KA, Overton IM, Dorward M, Liu H, McMahon SA, Oke M, Puech D, Barton GJ, Naismith JH, Campopiano DJ: The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis. J Mol Biol. 2007 Jul 27;370(5):870-86. Epub 2007 May 10. Pubmed: 17559874
    General function:
    Involved in catalytic activity
    Specific function:
    Catalyzes the last step in the biosynthesis of serine from carbohydrates. The reaction mechanism proceeds via the formation of a phosphoryl-enzyme intermediates.
    Gene Name:
    PSPH
    Uniprot ID:
    P78330
    Molecular weight:
    25007.49
    Reactions
    Phosphoserine + Water → L-Serine + Phosphoric aciddetails
    General function:
    Involved in transferase activity
    Specific function:
    Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC2-SPTSSA complex shows a strong preference for C16-CoA substrate, while the SPTLC1-SPTLC2-SPTSSB complex displays a preference for C18-CoA substrate.
    Gene Name:
    SPTLC2
    Uniprot ID:
    O15270
    Molecular weight:
    62923.765
    Reactions
    hexadecanoyl-CoA + L-Serine → Coenzyme A + 3-Dehydrosphinganine + CO(2)details
    hexadecanoyl-CoA + L-Serine → 3-Dehydrosphinganine + Coenzyme A + Carbon dioxidedetails
    References
    1. Yard BA, Carter LG, Johnson KA, Overton IM, Dorward M, Liu H, McMahon SA, Oke M, Puech D, Barton GJ, Naismith JH, Campopiano DJ: The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis. J Mol Biol. 2007 Jul 27;370(5):870-86. Epub 2007 May 10. Pubmed: 17559874
    General function:
    Involved in phosphatidylserine biosynthetic process
    Specific function:
    Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. In membranes, PTDSS1 catalyzes mainly the conversion of phosphatidylcholine. Also converts, in vitro and to a lesser extent, phosphatidylethanolamine.
    Gene Name:
    PTDSS1
    Uniprot ID:
    P48651
    Molecular weight:
    55527.18
    Reactions
    L-1-phosphatidylethanolamine + L-Serine → L-1-phosphatidylserine + Ethanolaminedetails
    General function:
    Involved in phosphatidylserine biosynthetic process
    Specific function:
    Catalyzes a base-exchange reaction in which the polar head group of phosphatidylethanolamine (PE) or phosphatidylcholine (PC) is replaced by L-serine. PTDSS2 is specific for phosphatatidylethanolamine and does not act on phosphatidylcholine.
    Gene Name:
    PTDSS2
    Uniprot ID:
    Q9BVG9
    Molecular weight:
    56252.55
    Reactions
    L-1-phosphatidylethanolamine + L-Serine → L-1-phosphatidylserine + Ethanolaminedetails
    General function:
    Involved in sodium:dicarboxylate symporter activity
    Specific function:
    Transporter for alanine, serine, cysteine, and threonine. Exhibits sodium dependence
    Gene Name:
    SLC1A4
    Uniprot ID:
    P43007
    Molecular weight:
    55722.5
    General function:
    Involved in catalytic activity
    Specific function:
    Has low serine dehydratase and threonine dehydratase activity.
    Gene Name:
    SDSL
    Uniprot ID:
    Q96GA7
    Molecular weight:
    34674.01
    Reactions
    L-Serine → Pyruvic acid + Ammoniadetails
    General function:
    Involved in transferase activity
    Specific function:
    Serine palmitoyltransferase (SPT). The heterodimer formed with LCB1/SPTLC1 constitutes the catalytic core. The composition of the serine palmitoyltransferase (SPT) complex determines the substrate preference. The SPTLC1-SPTLC3-SPTSSA isozyme uses both C14-CoA and C16-CoA as substrates, while the SPTLC1-SPTLC3-SPTSSB has the ability to use a broader range of acyl-CoAs without apparent preference.
    Gene Name:
    SPTLC3
    Uniprot ID:
    Q9NUV7
    Molecular weight:
    62049.035
    Reactions
    hexadecanoyl-CoA + L-Serine → Coenzyme A + 3-Dehydrosphinganine + CO(2)details
    hexadecanoyl-CoA + L-Serine → 3-Dehydrosphinganine + Coenzyme A + Carbon dioxidedetails
    General function:
    Involved in catalytic activity
    Specific function:
    Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.
    Gene Name:
    SRR
    Uniprot ID:
    Q9GZT4
    Molecular weight:
    36565.905
    Reactions
    L-Serine → D-Serinedetails
    L-Serine → Pyruvic acid + Ammoniadetails
    References
    1. Fujitani Y, Horiuchi T, Ito K, Sugimoto M: Serine racemases from barley, Hordeum vulgare L., and other plant species represent a distinct eukaryotic group: gene cloning and recombinant protein characterization. Phytochemistry. 2007 Jun;68(11):1530-6. Epub 2007 May 17. Pubmed: 17499824
    2. Ying-Luan Z, Zhao YL, Mori H: [Role of D-serine in the mammalian brain]. Brain Nerve. 2007 Jul;59(7):725-30. Pubmed: 17663143
    General function:
    Involved in catalytic activity
    Specific function:
    Interconversion of serine and glycine
    Gene Name:
    SHMT1
    Uniprot ID:
    A8MYA6
    Molecular weight:
    48998.5
    General function:
    Involved in catalytic activity
    Specific function:
    Interconversion of serine and glycine
    Gene Name:
    SHMT2
    Uniprot ID:
    Q5BJF5
    Molecular weight:
    52909.3
    General function:
    Involved in L-serine transmembrane transporter activity
    Specific function:
    Enhances the incorporation of serine into phosphatidylserine and sphingolipids
    Gene Name:
    SERINC1
    Uniprot ID:
    Q9NRX5
    Molecular weight:
    50494.4

    Transporters

    General function:
    Involved in transmembrane transport
    Specific function:
    Sodium-independent transporter that mediates the update of aromatic acid. Can function as a net efflux pathway for aromatic amino acids in the basosolateral epithelial cells
    Gene Name:
    SLC16A10
    Uniprot ID:
    Q8TF71
    Molecular weight:
    55492.1
    References
    1. Kim DK, Kanai Y, Chairoungdua A, Matsuo H, Cha SH, Endou H: Expression cloning of a Na+-independent aromatic amino acid transporter with structural similarity to H+/monocarboxylate transporters. J Biol Chem. 2001 May 18;276(20):17221-8. Epub 2001 Feb 20. Pubmed: 11278508