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Human Metabolome Database Version 2.5

 

Showing metabocard for Anserine (HMDB00194)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-04-12 15:55:44
Accession Number HMDB00194
Secondary Accession Numbers Not Available
Common Name Anserine
Description This dipeptide is normally absent from human tissues and body fluids, and its appearance there is an artifact of diet (Proc Soc Pediatr Res 134, 1967.) and serum carnosinase deficiency. (OMIM 212200) Anserine is present in the skeletal muscle of birds and certain species of mammals, notably the rabbit, rat, and whale, contains anserine. (Proc Soc Pediatr Res 134, 1967) The methyl group of anserine is added to carnosine by the enzyme S-adenosylmethionine: carnosine N-methyltransferase. (J Biol Chem 237:1207, 1962.)
Synonyms
  1. Anserine
  2. L-Anserine
  3. L-N-b-alanyl-3-methyl-Histidine
  4. N-b-alanyl-3-methyl-L-Histidine
  5. N-beta-Alanyl-3-methyl-L-histidine
  6. beta-alanyl-N(pai)-methyl-L-histidine
  7. L-N-beta-alanyl-3-methyl-Histidine
Chemical IUPAC Name 2-(3-aminopropanoylamino)-3-(3-methylimidazol-4-yl)-propanoic acid
Chemical Formula C10H16N4O3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Polypeptides
Sub Class
  • Dipeptides
Family
  • Mammalian Metabolite
Species
  • primary amine
  • primary aliphatic amine (alkylamine)
  • carboxylic acid
  • secondary carboxylic acid amide
  • aromatic compound
  • heterocyclic compound
Biofunction
Application
Source
  • Endogenous
Average Molecular Weight 240.259
Monoisotopic Molecular Weight 240.122238
Isomeric SMILES CN1C=NC=C1C[C@H](NC(=O)CCN)C(O)=O
Canonical SMILES CN1C=NC=C1CC(NC(=O)CCN)C(O)=O
KEGG Compound ID C01262 Link Image
BioCyc ID Not Available
BiGG ID Not Available
Wikipedia Link Anserine Link Image
NuGOwiki Link HMDB00194 Link Image
Metagene Link HMDB00194 Link Image
METLIN ID 5209 Link Image
PubChem Compound 112072 Link Image
PubChem Substance 10629587 Link Image
ChEBI ID 18323 Link Image
CAS Registry Number 584-85-0
InChI Identifier InChI=1/C10H16N4O3/c1-14-6-12-5-7(14)4-8(10(16)17)13-9(15)2-3-11/h5-6,8H,2-4,11H2,1H3,(H,13,15)(H,16,17)/t8-/m0/s1
Synthesis Reference Yudaev, N. A. Biosynthesis of anserine. Doklady Akademii Nauk SSSR (1952), 82 615-17.
Melting Point (Experimental) 226-228 oC
Experimental Water Solubility Not Available Source: PhysProp
Predicted Water Solubility 15.8 mg/mL [MEYLAN,WM et al. (1996)]; 4.01 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge 0
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -2.95 [Predicted by ALOGPS]; -3.8 [Predicted by PubChem via XLOGP]; -1.26 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show Link Image
SDF File Show Link Image
PDB File Show Link Image
2D Structure
3D Structure
Experimental PDB ID Not Available
Experimental 1H NMR Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Experimental 13C NMR Spectrum Not Available
Experimental 13C HSQC Spectrum Download Spectrum
Download FID (Bruker)
Show Experimental Conditions Link Image
Predicted 1H NMR Spectrum Show Image
Show Peaklist
Predicted 13C NMR Spectrum Show Image
Show Peaklist
Mass Spectrum
Low Energy
Download File
Show Experimental Conditions Link Image
Medium Energy
Download File
Show Experimental Conditions Link Image
High Energy
Download File
Show Experimental Conditions Link Image
Simplified TOCSY Spectrum Not Available
BMRB Spectrum Not Available
Cellular Location
  • Cytoplasm
Biofluid Location
  • Blood
  • Urine
Tissue Location
Tissue References
Brain
Muscle
Concentrations (Normal)
Biofluid Blood
Value 41.0 +/- 10.0 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Le Boucher J, Charret C, Coudray-Lucas C, Giboudeau J, Cynober L: Amino acid determination in biological fluids by automated ion-exchange chromatography: performance of Hitachi L-8500A. Clin Chem. 1997 Aug;43(8 Pt 1):1421-8. [PubMed Link Image]
Biofluid Urine
Value <5.921 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Doctor's Data
Biofluid Urine
Value 16.16 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Male
Patient information Normal
Comments Based on one experiment
References
  • Shaykhutdinov RA, MacInnis GD, Dowlatabadi R, Weljie AM, Vogel HJ. Quantitative analysis of metabolite concentrations in human urine samples using 13C{1H} NMR spectroscopy. Metabolomics. 2009
Concentrations (Abnormal)
Biofluid Blood
Value 0.457 +/- 0.214 uM
Age Elderly:>65 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • 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 Link Image]
Biofluid Urine
Value 8.0 +/- 5.0 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Alzheimer's disease
Comments Not Available
References
  • 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 Link Image]
Associated Disorders
Condition References
Alzheimer's disease
  • 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 Link Image]
OMIM ID
Pathways
Name SMPDB Link KEGG Link
Beta-Alanine Metabolism SMP00007 Link Image map00410 Link Image
General References
  1. Harris RC, Tallon MJ, Dunnett M, Boobis L, Coakley J, Kim HJ, Fallowfield JL, Hill CA, Sale C, Wise JA: The absorption of orally supplied beta-alanine and its effect on muscle carnosine synthesis in human vastus lateralis. Amino Acids. 2006 May;30(3):279-89. Epub 2006 Mar 24. [PubMed Link Image]
  2. Pagnano MW, Hanssen AD, Lewallen DG, Stuart MJ: Flexion instability after primary posterior cruciate retaining total knee arthroplasty. Clin Orthop Relat Res. 1998 Nov;(356):39-46. [PubMed Link Image]
  3. Abe H, Okuma E, Sekine H, Maeda A, Yoshiue S: Human urinary excretion of L-histidine-related compounds after ingestion of several meats and fish muscle. Int J Biochem. 1993 Sep;25(9):1245-9. [PubMed Link Image]
  4. Kang I, Han SW: Anserine bursitis in patients with osteoarthritis of the knee. South Med J. 2000 Feb;93(2):207-9. [PubMed Link Image]
  5. Magana Loarte JE, Perez Franco J, Sanchez Sanchez G: [Is therapy with local infiltrations feasible in primary care consultations?] Aten Primaria. 1999 Jan;23(1):4-7. [PubMed Link Image]
  6. Tan KM, Candlish JK: Carnosine and anserine as modulators of neutrophil function. Clin Lab Haematol. 1998 Aug;20(4):239-44. [PubMed Link Image]
  7. Boldyrev A, Abe H: Metabolic transformation of neuropeptide carnosine modifies its biological activity. Cell Mol Neurobiol. 1999 Feb;19(1):163-75. [PubMed Link Image]
  8. Wikipedia Link Image
Metabolic Enzymes
  1. Beta-Ala-His dipeptidase
Enzyme 1 [top]
Enzyme 1 ID 5713
Enzyme 1 Name Beta-Ala-His dipeptidase
Enzyme 1 Synonyms
  1. CNDP dipeptidase 1
  2. Carnosine dipeptidase 1
  3. Glutamate carboxypeptidase-like protein 2
  4. Serum carnosinase
Enzyme 1 Gene Name CNDP1
Enzyme 1 Protein Sequence >Beta-Ala-His dipeptidase
MDPKLGRMAASLLAVLLLLLERGMFSSPSPPPALLEKVFQYIDLHQDEFVQTLKEWVAIE
SDSVQPVPRFRQELFRMMAVAADTLQRLGARVASVDMGPQQLPDGQSLPIPPVILAELGS
DPTKGTVCFYGHLDVQPADRGDGWLTDPYVLTEVDGKLYGRGATDNKGPVLAWINAVSAF
RALEQDLPVNIKFIIEGMEEAGSVALEELVEKEKDRFFSGVDYIVISDNLWISQRKPAIT
YGTRGNSYFMVEVKCRDQDFHSGTFGGILHEPMADLVALLGSLVDSSGHILVPGIYDEVV
PLTEEEINTYKAIHLDLEEYRNSSRVEKFLFDTKEEILMHLWRYPSLSIHGIEGAFDEPG
TKTVIPGRVIGKFSIRLVPHMNVSAVEKQVTRHLEDVFSKRNSSNKMVVSMTLGLHPWIA
NIDDTQYLAAKRAIRTVFGTEPDMIRDGSTIPIAKMFQEIVHKSVVLIPLGAVDDGEHSQ
NEKINRWNYIEGTKLFAAFFLEMAQLH
Enzyme 1 Number of Residues 507
Enzyme 1 Molecular Weight 56691.6
Enzyme 1 Theoretical pI 4.95
Enzyme 1 GO Classification
Function
  • binding
  • catalytic activity
  • hydrolase activity
  • metallopeptidase activity
  • peptidase activity
  • peptidase activity, acting on L-amino acid peptides
  • protein binding
Process
  • macromolecule metabolic process
  • metabolic process
  • protein metabolic process
  • proteolysis
Component
Enzyme 1 General Function Involved in metallopeptidase activity
Enzyme 1 Specific Function Preferential hydrolysis of the beta-Ala-|-His dipeptide (carnosine), and also anserine, Xaa-|-His dipeptides and other dipeptides including homocarnosine
Enzyme 1 Pathways
Enzyme 1 Reactions
  • Preferential hydrolysis of the beta-Ala!His dipeptide (carnosine), and also anserine, Xaa!His dipeptides and other dipeptides including homocarnosine [RN:R01166 R03288] ALL_REAC R01166 R03288 COFACTOR Citrate [CPD:C00158]
  • Cadmium [CPD:C01413]
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-26
Enzyme 1 Transmembrane Regions
  • None
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 21071039 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q96KN2 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name CNDP1_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1524 bp
ATGGATCCCAAACTCGGGAGAATGGCTGCGTCCCTGCTGGCTGTGCTGCTGCTGCTGCTG
GAGCGCGGCATGTTCTCCTCACCCTCCCCGCCCCCGGCGCTGTTAGAGAAAGTCTTCCAG
TACATTGACCTCCATCAGGATGAATTTGTGCAGACGCTGAAGGAGTGGGTGGCCATCGAG
AGCGACTCTGTCCAGCCTGTGCCTCGCTTCAGACAAGAGCTCTTCAGAATGATGGCCGTG
GCTGCGGACACGCTGCAGCGCCTGGGGGCCCGTGTGGCCTCGGTGGACATGGGTCCTCAG
CAGCTGCCCGATGGTCAGAGTCTTCCAATACCTCCCGTCATCCTGGCCGAACTGGGGAGC
GATCCCACGAAAGGCACCGTGTGCTTCTACGGCCACTTGGACGTGCAGCCTGCTGACCGG
GGCGATGGGTGGCTCACGGACCCCTATGTGCTGACGGAGGTAGACGGGAAACTTTATGGA
CGAGGAGCGACCGACAACAAAGGCCCTGTCTTGGCTTGGATCAATGCTGTGAGCGCCTTC
AGAGCCCTGGAGCAAGATCTTCCTGTGAATATCAAATTCATCATTGAGGGGATGGAAGAG
GCTGGCTCTGTTGCCCTGGAGGAACTTGTGGAAAAAGAAAAGGACCGATTCTTCTCTGGT
GTGGACTACATTGTAATTTCAGATAACCTGTGGATCAGCCAAAGGAAGCCAGCAATCACT
TACGGAACCCGGGGGAACAGCTACTTCATGGTGGAGGTGAAATGCAGAGACCAGGATTTT
CACTCAGGAACCTTTGGTGGCATCCTTCATGAACCAATGGCTGATCTGGTTGCTCTTCTC
GGTAGCCTGGTAGACTCGTCTGGTCATATCCTGGTCCCTGGAATCTATGATGAAGTGGTT
CCTCTTACAGAAGAGGAAATAAATACATACAAAGCCATCCATCTAGACCTAGAAGAATAC
CGGAATAGCAGCCGGGTTGAGAAATTTCTGTTCGATACTAAGGAGGAGATTCTAATGCAC
CTCTGGAGGTACCCATCTCTTTCTATTCATGGGATCGAGGGCGCGTTTGATGAGCCTGGA
ACTAAAACAGTCATACCTGGCCGAGTTATAGGAAAATTTTCAATCCGTCTAGTCCCTCAC
ATGAATGTGTCTGCGGTGGAAAAACAGGTGACACGACATCTTGAAGATGTGTTCTCCAAA
AGAAATAGTTCCAACAAGATGGTTGTTTCCATGACTCTAGGACTACACCCGTGGATTGCA
AATATTGATGACACCCAGTATCTCGCAGCAAAAAGAGCGATCAGAACAGTGTTTGGAACA
GAACCAGATATGATCCGGGATGGATCCACCATTCCAATTGCCAAAATGTTCCAGGAGATC
GTCCACAAGAGCGTGGTGCTAATTCCGCTGGGAGCTGTTGATGATGGAGAACATTCGCAG
AATGAGAAAATCAACAGGTGGAACTACATAGAGGGAACCAAATTATTTGCTGCCTTTTTC
TTAGAGATGGCCCAGCTCCATTAA
Enzyme 1 GenBank Gene ID NM_032649.5 Link Image
Enzyme 1 GeneCard ID CNDP1 Link Image
Enzyme 1 GenAtlas ID CNDP1 Link Image
Enzyme 1 HGNC ID HGNC:20675 Link Image
Enzyme 1 Chromosome Location 1
Enzyme 1 Locus 18q22.3
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Janssen B, Hohenadel D, Brinkkoetter P, Peters V, Rind N, Fischer C, Rychlik I, Cerna M, Romzova M, de Heer E, Baelde H, Bakker SJ, Zirie M, Rondeau E, Mathieson P, Saleem MA, Meyer J, Koppel H, Sauerhoefer S, Bartram CR, Nawroth P, Hammes HP, Yard BA, Zschocke J, van der Woude FJ: Carnosine as a protective factor in diabetic nephropathy: association with a leucine repeat of the carnosinase gene CNDP1. Diabetes. 2005 Aug;54(8):2320-7. [PubMed Link Image]
  2. Clark HF, Gurney AL, Abaya E, Baker K, Baldwin D, Brush J, Chen J, Chow B, Chui C, Crowley C, Currell B, Deuel B, Dowd P, Eaton D, Foster J, Grimaldi C, Gu Q, Hass PE, Heldens S, Huang A, Kim HS, Klimowski L, Jin Y, Johnson S, Lee J, Lewis L, Liao D, Mark M, Robbie E, Sanchez C, Schoenfeld J, Seshagiri S, Simmons L, Singh J, Smith V, Stinson J, Vagts A, Vandlen R, Watanabe C, Wieand D, Woods K, Xie MH, Yansura D, Yi S, Yu G, Yuan J, Zhang M, Zhang Z, Goddard A, Wood WI, Godowski P, Gray A: The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment. Genome Res. 2003 Oct;13(10):2265-70. Epub 2003 Sep 15. [PubMed Link Image]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed Link Image]
  4. Lenney JF, George RP, Weiss AM, Kucera CM, Chan PW, Rinzler GS: Human serum carnosinase: characterization, distinction from cellular carnosinase, and activation by cadmium. Clin Chim Acta. 1982 Aug 18;123(3):221-31. [PubMed Link Image]
  5. Lenney JF, Peppers SC, Kucera CM, Sjaastad O: Homocarnosinosis: lack of serum carnosinase is the defect probably responsible for elevated brain and CSF homocarnosine. Clin Chim Acta. 1983 Aug 15;132(2):157-65. [PubMed Link Image]
  6. Teufel M, Saudek V, Ledig JP, Bernhardt A, Boularand S, Carreau A, Cairns NJ, Carter C, Cowley DJ, Duverger D, Ganzhorn AJ, Guenet C, Heintzelmann B, Laucher V, Sauvage C, Smirnova T: Sequence identification and characterization of human carnosinase and a closely related non-specific dipeptidase. J Biol Chem. 2003 Feb 21;278(8):6521-31. Epub 2002 Dec 6. [PubMed Link Image]
  7. Liu T, Qian WJ, Gritsenko MA, Camp DG 2nd, Monroe ME, Moore RJ, Smith RD: Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J Proteome Res. 2005 Nov-Dec;4(6):2070-80. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available