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Human Metabolome Database Version 2.5

 

Showing metabocard for Pyroglutamic acid (HMDB00267)

Legend: metabolite field enzyme field

Version 2.5
Creation Date 2005-11-16 15:48:42
Update Date 2010-07-12 12:04:55
Accession Number HMDB00267
Secondary Accession Numbers Not Available
Common Name Pyroglutamic acid
Description A cyclized derivative of L-glutamic acid. It is an uncommon amino acid derivative in which the free amino group of glutamic acid cyclizes to form a lactam. It is formed nonenzymatically from glutamate, glutamine, and gamma-glutamylated peptides, but it can also be produced by the action of gamma-glutamylcyclotransferase on an L-amino acid. Elevated blood levels may be associated with problems of glutamine or glutathione metabolism. This compound is found in substantial amounts in brain tissue and other tissue in bound form, esp. skin. Also present in plant tissues. It is sold, over the counter, as a "smart drug" for improving blood circulation in the brain.
Synonyms
  1. (-)-2-Pyrrolidone-5-carboxylate
  2. (-)-2-Pyrrolidone-5-carboxylic acid
  3. (-)-Pyroglutamate
  4. (-)-Pyroglutamic acid
  5. (5S)-2-Oxopyrrolidine-5-carboxylate
  6. (5S)-2-Oxopyrrolidine-5-carboxylic acid
  7. (S)-(-)-2-Pyrrolidone-5-carboxylate
  8. (S)-(-)-2-Pyrrolidone-5-carboxylic acid
  9. (S)-(-)-g-Butyrolactam-g-carboxylate
  10. (S)-(-)-g-Butyrolactam-g-carboxylic acid
  11. (S)-2-Pyrrolidone-5-carboxylate
  12. (S)-2-Pyrrolidone-5-carboxylic acid
  13. (S)-5-Oxo-2-pyrrolidinecarboxylate
  14. (S)-5-Oxo-2-pyrrolidinecarboxylic acid
  15. (S)-Pyroglutamate
  16. (S)-Pyroglutamic acid
  17. 2-L-Pyrrolidone-5-carboxylate
  18. 2-L-Pyrrolidone-5-carboxylic acid
  19. 2-Oxopyrrolidine-5(S)-carboxylate
  20. 2-Oxopyrrolidine-5(S)-carboxylic acid
  21. 2-Pyrrolidinone-5-carboxylate
  22. 2-Pyrrolidinone-5-carboxylic acid
  23. 5-Carboxy-2-pyrrolidinone
  24. 5-Oxo-L-proline
  25. 5-L-oxoproline
  26. 5-Oxoproline
  27. 5-Pyrrolidinone-2-carboxylate
  28. 5-Pyrrolidinone-2-carboxylic acid
  29. Ajidew A 100
  30. Glutimate
  31. Glutimic acid
  32. Glutiminate
  33. Glutiminic acid
  34. L-2-Pyrrolidone-5-carboxylate
  35. L-2-Pyrrolidone-5-carboxylic acid
  36. L-5-Carboxy-2-pyrrolidinone
  37. L-5-Oxo-2-pyrrolidinecarboxylate
  38. L-5-Oxo-2-pyrrolidinecarboxylic acid
  39. L-5-Oxoproline
  40. L-Glutamic acid g-lactam
  41. L-Glutimate
  42. L-Glutimic acid
  43. L-Glutiminate
  44. L-Glutiminic acid
  45. L-Pyroglutamate
  46. L-Pyroglutamic acid
  47. L-Pyrrolidinonecarboxylate
  48. L-Pyrrolidinonecarboxylic acid
  49. L-Pyrrolidonecarboxylate
  50. L-Pyrrolidonecarboxylic acid
  51. Oxoproline
  52. Oxopyrrolidinecarboxylate
  53. Oxopyrrolidinecarboxylic acid
  54. Pidolate
  55. Pidolic acid
  56. Pidolidone
  57. Pyroglutamate
  58. Pyroglutamic acid
  59. Pyrrolidinonecarboxylate
  60. Pyrrolidinonecarboxylic acid
  61. Pyrrolidone-5-carboxylate
  62. Pyrrolidone-5-carboxylic acid
  63. Pyrrolidonecarboxylic acid
  64. (S)-(-)-gamma-Butyrolactam-gamma-carboxylate
  65. (S)-(-)-gamma-Butyrolactam-gamma-carboxylic acid
Chemical IUPAC Name (2S)-5-oxopyrrolidine-2-carboxylic acid
Chemical Formula C5H7NO3
Chemical Structure Structure
Chemical Taxonomy
Kingdom
  • Organic
Super Class
  • Amino acids and Amino Acid conjugates
Class
  • Amino Acids
  • Amino Ketones
Sub Class
  • NA
Family
  • Mammalian Metabolite
Species
  • carboxylic acid
  • secondary carboxylic acid amide
  • lactam
  • heterocyclic compound
Biofunction
  • Essential amino acid
  • Component of Glutathione metabolism
Application
—
Source
  • Endogenous
Average Molecular Weight 129.114
Monoisotopic Molecular Weight 129.042587
Isomeric SMILES OC(=O)[C@@H]1CCC(=O)N1
Canonical SMILES OC(=O)C1CCC(=O)N1
KEGG Compound ID C01879 Link Image
BioCyc ID CPD-589 Link Image
BiGG ID 1800372 Link Image
Wikipedia Link Pyroglutamic acid Link Image
NuGOwiki Link HMDB00267 Link Image
Metagene Link HMDB00267 Link Image
METLIN ID 3251 Link Image
PubChem Compound 7405 Link Image
PubChem Substance 76605 Link Image
ChEBI ID 18183 Link Image
CAS Registry Number 98-79-3
InChI Identifier InChI=1/C5H7NO3/c7-4-2-1-3(6-4)5(8)9/h3H,1-2H2,(H,6,7)(H,8,9)/t3-/m0/s1
Synthesis Reference Pumpor, Ksenia; Boettcher, Christoph; Fehn, Susanna; Burger, Klaus. Hexafluoroacetone as protecting and activating reagent: an efficient strategy for activation of pyroglutamic acid and homologs.Heterocycles (2003), 61 259-269.
Melting Point (Experimental) Not Available
Experimental Water Solubility 476.0 mg/mL at 13 oC [BEILSTEIN] Source: PhysProp
Predicted Water Solubility 151.0 mg/mL [Predicted by ALOGPS] Calculated using ALOGPS
Physiological Charge -1
State Solid
Experimental LogP/Hydrophobicity Not Available Source: PhysProp
Predicted LogP/Hydrophobicity -1.01 [Predicted by ALOGPS]; -3 [Predicted by PubChem via XLOGP]; -0.72 [MEYLAN,WM & HOWARD,PH (1995)] Calculated using ALOGPS
Material Safety Data Sheet (MSDS)
MOL File Show
SDF File Show
PDB File Show
2D Structure
3D Structure
Experimental PDB ID 1A8J Link Image
Experimental PDB File Show
Experimental PDB Structure
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 (Predicted from LogP)
Biofluid Location
  • Blood
  • Cerebrospinal Fluid
  • Urine
Tissue Location
Tissue References
Brain —
Skin —
Concentrations (Normal)
Biofluid Blood
Value 19.5 +/- 3.7 uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Friesen RW, Novak EM, Hasman D, Innis SM: Relationship of dimethylglycine, choline, and betaine with oxoproline in plasma of pregnant women and their newborn infants. J Nutr. 2007 Dec;137(12):2641-6. [PubMed Link Image]
Biofluid Blood
Value 87.00 (13.00-161.00) uM
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Biofluid CSF
Value 41.0 +/- 31.0 uM
Age Adult:>18 yrs old
Sex N/A
Patient information Normal
Comments Not Available
References
  • Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
Biofluid CSF
Value 47 +/- 30 uM
Age N/A
Sex Both
Patient information Normal
Comments Not Available
References
  • Wishart DS, Lewis MJ, Morrissey JA, Flegel MD, Jeroncic K, Xiong Y, Cheng D, Eisner R, Gautam B, Tzur D, Sawhney S, Bamforth F, Greiner R, Li L: The human cerebrospinal fluid metabolome. J Chromatogr B Analyt Technol Biomed Life Sci. 2008 Aug 15;871(2):164-173. Epub 2008 May 8. [PubMed Link Image]
Biofluid Urine
Value 7.3 (0.1-29.3) umol/mmol creatinine
Age Newborn:0-30 days old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 24.1 (3.4-54.2) umol/mmol creatinine
Age Infant:0-1 yr old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 5.3 (2.9-10.4) umol/mmol creatinine
Age Children:1-13 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 3.1 (1.9-11.3) umol/mmol creatinine
Age Adolescent:13-18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
  • Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
Biofluid Urine
Value 28.8 (3.4-54.2) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Patient information Normal
Comments Not Available
References
Concentrations (Abnormal)
Biofluid Blood
Value 3.5 (3.00-4.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Glutathione synthetase deficiency
Comments Not Available
References
Biofluid CSF
Value 2326.0 uM
Age Adult:>18 yrs old
Sex Both
Condition Glutathione synthetase deficiency
Comments Not Available
References
  • Jellum E, Stokke O, Eldjarn L: Combined use of gas chromatography, mass spectrometry, and computer in diagnosis and studies of metabolic disorders. Clin Chem. 1972 Aug;18(8):800-9. [PubMed Link Image]
Biofluid Urine
Value 1.9 umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Glutathione synthetase deficiency
Comments Not Available
References
  • Wevers RA, Engelke U, Heerschap A: High-resolution 1H-NMR spectroscopy of blood plasma for metabolic studies. Clin Chem. 1994 Jul;40(7 Pt 1):1245-50. [PubMed Link Image]
Biofluid Urine
Value 3500.0 (1000.0-6000.0) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Comments Not Available
References
Biofluid Urine
Value 17000.00 (4000.00-30000.00) umol/mmol creatinine
Age Adult:>18 yrs old
Sex Both
Condition Glutathione synthetase deficiency
Comments Not Available
References
Associated Disorders
Condition References
Glutathione synthetase deficiency
OMIM ID
  • 266130 Link Image (Glutathione synthetase deficiency)
Pathways
Name SMPDB Link KEGG Link
Glutathione Metabolism SMP00015 Link Image map00480 Link Image
General References
  1. Manning NJ, Davies NP, Olpin SE, Carpenter KH, Smith MF, Pollitt RJ, Duncan SL, Larsson A, Carlsson B: Prenatal diagnosis of glutathione synthase deficiency. Prenat Diagn. 1994 Jun;14(6):475-8. [PubMed Link Image]
  2. Caspers PJ, Lucassen GW, Carter EA, Bruining HA, Puppels GJ: In vivo confocal Raman microspectroscopy of the skin: noninvasive determination of molecular concentration profiles. J Invest Dermatol. 2001 Mar;116(3):434-42. [PubMed Link Image]
  3. Hussain Z, Lannigan R, Stoakes L: A new approach for presumptive identification of clinically important streptococci. Zentralbl Bakteriol Mikrobiol Hyg [A]. 1984 Oct;258(1):74-9. [PubMed Link Image]
  4. Guneral F, Bachmann C: Age-related reference values for urinary organic acids in a healthy Turkish pediatric population. Clin Chem. 1994 Jun;40(6):862-6. [PubMed Link Image]
  5. Creer MH, Lau BW, Jones JD, Chan KM: Pyroglutamic acidemia in an adult patient. Clin Chem. 1989 Apr;35(4):684-6. [PubMed Link Image]
  6. Hammond JW, Potter M, Truscott R, Wilcken B: gamma-Glutamylglutamine identified in plasma and cerebrospinal fluid from hyperammonaemic patients. Clin Chim Acta. 1990 Dec 24;194(2-3):173-83. [PubMed Link Image]
  7. Uhlhaas S, Lange H: Striatal deficiency of L-pyroglutamic acid in Huntington's disease is accompanied by increased plasma levels. Brain Res. 1988 Aug 2;457(1):196-9. [PubMed Link Image]
  8. Jellum E, Stokke O, Eldjarn L: Combined use of gas chromatography, mass spectrometry, and computer in diagnosis and studies of metabolic disorders. Clin Chem. 1972 Aug;18(8):800-9. [PubMed Link Image]
  9. Croal BL, Glen AC, Kelly CJ, Logan RW: Transient 5-oxoprolinuria (pyroglutamic aciduria) with systemic acidosis in an adult receiving antibiotic therapy. Clin Chem. 1998 Feb;44(2):336-40. [PubMed Link Image]
  10. Winslow JW, Shih A, Bourell JH, Weiss G, Reed B, Stults JT, Goldsmith LT: Human seminal relaxin is a product of the same gene as human luteal relaxin. Endocrinology. 1992 May;130(5):2660-8. [PubMed Link Image]
  11. Hoffmann GF, Meier-Augenstein W, Stockler S, Surtees R, Rating D, Nyhan WL: Physiology and pathophysiology of organic acids in cerebrospinal fluid. J Inherit Metab Dis. 1993;16(4):648-69. [PubMed Link Image]
  12. Wevers RA, Engelke U, Heerschap A: High-resolution 1H-NMR spectroscopy of blood plasma for metabolic studies. Clin Chem. 1994 Jul;40(7 Pt 1):1245-50. [PubMed Link Image]
  13. Erasmus E, Mienie LJ, de Vries WN, de Wet WJ, Carlsson B, Larsson A: Prenatal analysis in two suspected cases of glutathione synthetase deficiency. J Inherit Metab Dis. 1993;16(5):837-43. [PubMed Link Image]
  14. Wikipedia Link Image
Metabolic Enzymes
  1. Glutaminyl-peptide cyclotransferase precursor
  2. 5-oxoprolinase
  3. 5-oxoprolinase
  4. Gamma-glutamylcyclotransferase
Enzyme 1 [top]
Enzyme 1 ID 5965
Enzyme 1 Name Glutaminyl-peptide cyclotransferase precursor
Enzyme 1 Synonyms
  1. QC
  2. Glutaminyl-tRNA cyclotransferase
  3. Glutaminyl cyclase
Enzyme 1 Gene Name QPCT
Enzyme 1 Protein Sequence >Glutaminyl-peptide cyclotransferase precursor 
MAGGRHRRVVGTLHLLLLVAALPWASRGVSPSASAWPEEKNYHQPAILNSSALRQIAEGT
SISEMWQNDLQPLLIERYPGSPGSYAARQHIMQRIQRLQADWVLEIDTFLSQTPYGYRSF
SNIISTLNPTAKRHLVLACHYDSKYFSHWNNRVFVGATDSAVPCAMMLELARALDKKLLS
LKTVSDSKPDLSLQLIFFDGEEAFLHWSPQDSLYGSRHLAAKMASTPHPPGARGTSQLHG
MDLLVLLDLIGAPNPTFPNFFPNSARWFERLQAIEHELHELGLLKDHSLEGRYFQNYSYG
GVIQDDHIPFLRRGVPVLHLIPSPFPEVWHTMDDNEENLDESTIDNLNKILQVFVLEYLH
L
Enzyme 1 Number of Residues 361
Enzyme 1 Molecular Weight 40877
Enzyme 1 Theoretical pI 6.60
Enzyme 1 GO Classification
Function
  • catalytic activity
  • hydrolase activity
  • peptidase activity
Process
  • cellular protein metabolism
  • macromolecule metabolism
  • metabolism
  • physiological process
  • protein metabolism
  • proteolysis
Component
—
Enzyme 1 General Function Not Available
Enzyme 1 Specific Function Responsible for the biosynthesis of pyroglutamyl peptides. Has a bias against acidic and tryptophan residues adjacent to the N-terminal glutaminyl residue and a lack of importance of chain length after the second residue
Enzyme 1 Pathways Not Available
Enzyme 1 Reactions
  • L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH3
Enzyme 1 Pfam Domain Function
Enzyme 1 Signals
  • 1-28
Enzyme 1 Transmembrane Regions Not Available
Enzyme 1 Essentiality Not Available
Enzyme 1 GenBank ID Protein 296949 Link Image
Enzyme 1 UniProtKB/Swiss-Prot ID Q16769 Link Image
Enzyme 1 UniProtKB/Swiss-Prot Entry Name QPCT_HUMAN Link Image
Enzyme 1 PDB ID Not Available
Enzyme 1 Cellular Location Not Available
Enzyme 1 Gene Sequence >1086 bp 
ATGGCAGGCGGAAGACACCGGCGCGTCGTGGGCACCCTCCACCTGCTGCTGCTGGTGGCC
GCCCTGCCCTGGGCATCCAGGGGGGTCAGTCCGAGTGCCTCAGCCTGGCCAGAGGAGAAG
AATTACCACCAGCCAGCCATTTTGAATTCATCGGCTCTTCGGCAAATTGCAGAAGGCACC
AGTATCTCTGAAATGTGGCAAAATGACTTACAGCCATTGCTGATAGAGCGATACCCGGGA
TCCCCTGGAAGCTATGCTGCTCGTCAGCACATCATGCAGCGAATTCAGAGGCTTCAGGCT
GACTGGGTCTTGGAAATAGACACCTTCTTGAGTCAGACACCCTATGGGTACCGGTCTTTC
TCAAATATCATCAGCACCCTCAATCCCACTGCTAAACGACATTTGGTCCTCGCCTGCCAC
TATGACTCCAAGTATTTTTCCCACTGGAACAACAGAGTGTTTGTAGGAGCCACTGATTCA
GCCGTGCCATGTGCAATGATGTTGGAACTTGCTCGTGCCTTAGACAAGAAACTCCTTTCC
TTAAAGACTGTTTCAGACTCCAAGCCAGATTTGTCACTCCAGCTGATCTTCTTTGATGGT
GAAGAGGCTTTTCTTCACTGGTCTCCTCAAGATTCTCTCTATGGGTCTCGACACTTAGCT
GCAAAGATGGCATCGACCCCGCACCCACCTGGAGCGAGAGGCACCAGCCAACTGCATGGC
ATGGATTTATTGGTCTTATTGGATTTGATTGGAGCTCCAAACCCAACGTTTCCCAATTTT
TTTCCAAACTCAGCCAGGTGGTTCGAAAGACTTCAAGCAATTGAACATGAACTTCATGAA
TTGGGTTTGCTCAAGGATCACTCTTTGGAGGGGCGGTATTTCCAGAATTACAGTTATGGA
GGTGTGATTCAGGATGACCATATTCCATTTTTAAGAAGAGGTGTTCCAGTTCTGCATCTG
ATACCGTCTCCTTTCCCTGAAGTCTGGCACACCATGGATGACAATGAAGAAAATTTGGAT
GAATCAACCATTGACAATCTAAACAAAATCCTACAAGTCTTTGTGTTGGAATATCTTCAT
TTGTAA
Enzyme 1 GenBank Gene ID X71125 Link Image
Enzyme 1 GeneCard ID QPCT Link Image
Enzyme 1 GenAtlas ID QPCT Link Image
Enzyme 1 HGNC ID HGNC:9753 Link Image
Enzyme 1 Chromosome Location 2
Enzyme 1 Locus 2p22.2
Enzyme 1 SNPs SNPJam Report Link Image
Enzyme 1 General References
  1. Song I, Chuang CZ, Bateman RC Jr: Molecular cloning, sequence analysis and expression of human pituitary glutaminyl cyclase. J Mol Endocrinol. 1994 Aug;13(1):77-86. [PubMed Link Image]
Enzyme 1 Metabolite References Not Available
Enzyme 2 [top]
Enzyme 2 ID 6136
Enzyme 2 Name 5-oxoprolinase
Enzyme 2 Synonyms
  1. 5-oxo-L-prolinase
  2. Pyroglutamase
  3. 5- OPase
Enzyme 2 Gene Name OPLAH
Enzyme 2 Protein Sequence >5-oxoprolinase 
MGSPEGRFHFAIDRGGTFTDVFAQCPGGHVRVLKLLSEDPANYADAPTEGIRRILEQEAG
MLLPRDQPLDSSHIASIRMGTTVATNALLERKGERVALLVTRGFRDLLHIGTQARGDLFD
LAVPMPEVLYEEVLEVDERVVLHRGEAGTGTPVKGRTGDLLEVQQPVDLGALRGKLEGLL
SRGIRSLAVVLMHSYTWAQHEQQVGVLARELGFTHVSLSSEAMPMVRIVPRGHTACADAY
LTPAIQRYVQGFCRGFQGQLKDVQVLFMRSDGGLAPMDTFSGSSAVLSGPAGGVVGYSAT
TYQQEGGQPVIGFDMGGTSTDVSRYAGEFEHVFEASTAGVTLQAPQLDINTVAAGGGSRL
FFRSGLFVVGPESAGAHPGPACYRKGGPVTVTDANLVLGRLLPASFPCIFGPGENQPLSP
EASRKALEAVATEVNSFLTNGPCPASPLSLEEVAMGFVRVANEAMCRPIRALTQARGHDP
SAHVLACFGGAGGQHACAIARALGMDTVHIHRHSGLLSALGLALADVVHEAQEPCSLLYA
PETFVQLDQRLSRLEEQCVDALQAQGFPRSQISTESFLHLRYQGTDCALMVSAHQHPATA
RSPRAGDFGAAFVERYMREFGFVIPERPVVVDDVRVRGTGRSGLRLEDAPKAQTGPPRVD
KMTQCYFEGGYQETPVYLLAELGYGHKLHGPCLIIDSNSTILVEPGCQAEVTKTGDICIS
VGAEVPGTVGPQLDPIQLSIFSHRFMSIAEQMGRILQRTAISTNIKERLDFSCALFGPDG
GLVSNAPHIPVHLGAMQETVQFQIQHLGADLHPGDVLLSNHPSAGGSHLPDLTVITPVFW
PGQTRPVFYVASRGHHADIGGITPGSMPPHSTMLQQEGAVFLSFKLVQGGVFQEEAVTEA
LRAPGKVPNCSGTRNLHDNLSDLRAQVAANQKGIQLVGELIGQYGLDVVQAYMGHIQANA
ELAVRDMLRAFGTSRQARGLPLEVSSEDHMDDGSPIRLRVQISLSQGSAVFDFSGTGPEV
FGNLNAPRAVTLSALIYCLRCLVGRDIPLNQGCLAPVRVVIPRGSILDPSPEAAVVGGNV
LTSQRVVDVILGAFGACAASQGCMNNVTLGNAHMGYYETVAGGAGAGPSWHGRSGVHSHM
TNTRITDPEILESRYPVILRRFELRRGSGGRGRFRGGDGVTRELLFREEALLSVLTERRA
FRPYGLHGGEPGARGLNLLIRKNGRTVNLGGKTSVTVYPGDVFCLHTPGGGGYGDPEDPA
PPPGSPPQALAFPEHGSVYEYRRAQEAV
Enzyme 2 Number of Residues 1288
Enzyme 2 Molecular Weight 137459
Enzyme 2 Theoretical pI 6.56
Enzyme 2 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 2 General Function Amino acid transport and metabolism
Enzyme 2 Specific Function Catalyzes the cleavage of 5-oxo-L-proline to form L- glutamate coupled to the hydrolysis of ATP to ADP and inorganic phosphate
Enzyme 2 Pathways
Enzyme 2 Reactions
  • ATP + 5-oxo-L-proline + 2 H2O = ADP + phosphate + L-glutamate
Enzyme 2 Pfam Domain Function
Enzyme 2 Signals
  • None
Enzyme 2 Transmembrane Regions
  • None
Enzyme 2 Essentiality Not Available
Enzyme 2 GenBank ID Protein 46020040 Link Image
Enzyme 2 UniProtKB/Swiss-Prot ID O14841 Link Image
Enzyme 2 UniProtKB/Swiss-Prot Entry Name OPLA_HUMAN Link Image
Enzyme 2 PDB ID Not Available
Enzyme 2 Cellular Location Not Available
Enzyme 2 Gene Sequence >3867 bp 
ATGGGCAGCCCCGAGGGCCGCTTCCACTTTGCCATCGACCGTGGGGGTACCTTCACAGAC
GTCTTTGCCCAGTGCCCAGGGGGGCACGTGCGGGTCTTAAAACTGCTCTCAGAGGACCCT
GCCAACTATGCGGACGCGCCAACCGAAGGCATCCGCCGCATCCTGGAGCAGGAGGCCGGC
ATGCTCCTGCCCCGGGACCAGCCGCTGGACTCCAGTCATATCGCCAGCATCCGCATGGGC
ACCACAGTGGCCACCAACGCACTGCTGGAGCGGAAGGGGGAGCGGGTGGCGCTGCTGGTG
ACACGTGGCTTCCGAGACCTGCTGCACATTGGCACCCAAGCCCGTGGGGACCTCTTTGAC
CTGGCCGTGCCCATGCCTGAGGTGCTGTATGAAGAGGTGCTGGAGGTGGACGAACGCGTG
GTGCTGCACCGTGGAGAGGCGGGCACCGGGACGCCTGTGAAAGGCCGCACGGGGGACCTG
CTGGAAGTGCAGCAGCCTGTGGACCTGGGGGCCCTGCGTGGGAAGCTGGAGGGGCTGCTA
TCTCGAGGCATCCGCAGCCTGGCTGTGGTGCTCATGCACTCGTACACGTGGGCCCAGCAT
GAGCAGCAGGTGGGTGTGCTGGCCCGGGAGCTGGGCTTCACGCACGTGTCACTGTCCTCG
GAGGCCATGCCCATGGTGCGCATCGTCCCTCGGGGGCACACGGCCTGTGCCGACGCCTAC
CTCACGCCCGCCATCCAGCGCTACGTGCAGGGCTTCTGCCGTGGCTTCCAGGGCCAACTC
AAGGATGTGCAGGTGTTGTTCATGCGCTCCGATGGCGGCCTGGCGCCCATGGACACCTTC
AGCGGCTCCAGTGCTGTGCTCTCGGGCCCGGCCGGCGGCGTGGTGGGCTACTCAGCCACC
ACCTACCAGCAGGAGGGTGGCCAGCCTGTCATCGGCTTTGACATGGGAGGCACGTCCACG
GATGTGAGCCGCTATGCTGGGGAATTCGAGCACGTCTTCGAGGCCAGCACAGCTGGCGTC
ACCCTCCAGGCCCCGCAGCTGGACATCAACACCGTGGCAGCGGGAGGGGGTTCCCGCCTC
TTCTTCAGGTCTGGCCTCTTTGTGGTTGGGCCCGAGTCAGCAGGAGCCCACCCAGGACCC
GCCTGCTACCGCAAAGGGGGCCCTGTGACAGTGACGGATGCTAATCTGGTCCTGGGTCGC
CTGCTGCCTGCCTCCTTCCCCTGCATTTTTGGGCCGGGAGAGAACCAACCACTTTCCCCT
GAGGCCTCCCGCAAAGCCCTGGAGGCTGTGGCCACTGAGGTCAACAGCTTCCTGACCAAC
GGGCCCTGCCCGGCCTCCCCGCTGAGCCTGGAGGAGGTGGCCATGGGGTTCGTGCGCGTG
GCCAACGAGGCCATGTGCCGGCCCATCCGTGCACTCACGCAGGCAAGAGGCCATGACCCC
TCAGCCCATGTGCTGGCCTGCTTTGGGGGAGCTGGTGGGCAGCATGCATGTGCCATCGCC
CGGGCCCTGGGCATGGACACGGTGCACATCCACAGGCACAGTGGGCTGCTGTCGGCCCTG
GGGCTGGCCCTGGCTGACGTGGTGCATGAGGCACAGGAACCCTGCTCCCTGCTCTACGCG
CCTGAGACCTTCGTGCAGCTGGACCAGAGGCTGAGCCGCCTGGAGGAGCAGTGTGTGGAT
GCTCTGCAGGCCCAGGGCTTCCCCAGGTCCCAGATCAGCACTGAGAGCTTCCTGCACCTG
CGCTACCAGGGCACGGACTGTGCTCTGATGGTGTCTGCCCACCAGCACCCAGCCACAGCC
CGCTCGCCCCGTGCGGGGGACTTCGGGGCAGCCTTTGTGGAGCGGTACATGAGGGAGTTT
GGCTTTGTCATACCTGAGCGGCCGGTGGTCGTGGACGATGTGCGAGTGCGGGGCACCGGC
CGCAGTGGTCTTCGCCTCGAGGATGCCCCCAAAGCCCAGACCGGGCCTCCCCGGGTGGAC
AAGATGACCCAGTGCTACTTTGAGGGGGGCTACCAGGAGACCCCTGTGTACCTGCTGGCA
GAGCTGGGCTATGGGCACAAGCTCCATGGGCCCTGCCTCATCATCGACAGTAACAGCACC
ATCCTGGTGGAGCCAGGTTGCCAGGCAGAGGTGACCAAGACAGGGGACATCTGCATCTCC
GTGGGGGCCGAAGTCCCCGGCACAGTGGGCCCCCAGCTGGACCCTATCCAGCTGTCCATC
TTCTCACACCGCTTCATGAGCATTGCTGAGCAGATGGGCCGCATCCTGCAGCGCACAGCC
ATCTCCACCAACATCAAGGAGCGTCTGGACTTCTCCTGTGCCCTCTTTGGGCCCGATGGG
GGGCTGGTGTCCAATGCCCCCCACATCCCTGTGCACCTGGGTGCCATGCAGGAGACGGTG
CAGTTCCAGATTCAGCACCTGGGGGCCGATCTCCACCCTGGCGACGTGCTACTGAGCAAC
CATCCCAGTGCCGGGGGCAGCCACCTGCCAGACCTGACTGTTATCACACCGGTGTTTTGG
CCGGGTCAGACGCGGCCTGTGTTCTATGTGGCCAGCCGAGGGCACCACGCAGACATCGGG
GGCATCACACCAGGCTCCATGCCCCCCCACTCCACCATGCTGCAACAGGAGGGTGCCGTC
TTTCTGTCCTTCAAACTTGTCCAGGGGGGCGTCTTCCAGGAGGAGGCGGTGACGGAGGCC
CTGCGGGCGCCAGGCAAGGTCCCCAACTGCAGCGGAACCAGAAACCTGCACGACAACCTG
TCGGACCTCCGTGCCCAGGTGGCAGCCAACCAGAAGGGCATCCAGCTGGTGGGGGAGCTC
ATTGGGCAGTACGGCCTGGACGTGGTGCAGGCCTACATGGGCCATATTCAGGCAAACGCT
GAGCTGGCCGTGCGAGACATGTTGCGTGCCTTTGGAACCTCCCGGCAGGCCCGGGGCCTG
CCCCTGGAGGTGTCCTCGGAAGACCACATGGACGACGGTTCCCCCATCCGCCTCCGTGTG
CAGATCAGCCTGAGTCAGGGCAGCGCTGTGTTTGACTTCAGCGGCACTGGGCCGGAGGTG
TTTGGTAATCTCAACGCACCGCGGGCCGTAACCCTGTCCGCCCTCATCTACTGCCTGCGC
TGTCTGGTGGGCCGCGACATCCCACTCAACCAGGGCTGCCTGGCGCCAGTGCGCGTGGTC
ATTCCCCGAGGCTCCATCCTGGACCCGTCGCCCGAGGCGGCGGTGGTGGGCGGCAACGTG
CTCACGTCGCAGCGCGTGGTGGATGTCATCCTGGGGGCCTTTGGGGCCTGCGCCGCCTCC
CAGGGCTGCATGAACAACGTGACCCTGGGCAACGCCCACATGGGCTACTACGAGACGGTG
GCGGGCGGCGCGGGCGCGGGTCCCAGCTGGCACGGGCGCAGCGGTGTGCACAGCCACATG
ACCAACACACGCATCACCGACCCTGAGATCCTGGAGAGCCGGTACCCGGTCATCCTGCGC
CGCTTCGAGCTGCGGCGGGGCTCGGGGGGCAGAGGCCGCTTCCGAGGCGGCGACGGCGTC
ACCCGCGAGCTGCTCTTTCGTGAGGAGGCGCTGCTGTCAGTGCTGACCGAGCGCCGCGCC
TTCCGGCCATACGGGCTCCACGGGGGCGAGCCTGGCGCCCGCGGCCTAAACCTGCTGATC
CGCAAAAACGGCCGGACGGTGAATCTGGGCGGCAAGACGTCGGTGACCGTGTACCCCGGG
GATGTGTTCTGTCTCCACACGCCCGGCGGCGGTGGCTATGGGGACCCGGAGGACCCCGCC
CCACCGCCGGGGTCGCCCCCGCAAGCACTGGCCTTTCCCGAGCACGGCAGCGTCTATGAG
TATCGCCGGGCCCAGGAGGCCGTGTGA
Enzyme 2 GenBank Gene ID AB122018 Link Image
Enzyme 2 GeneCard ID OPLAH Link Image
Enzyme 2 GenAtlas ID OPLAH Link Image
Enzyme 2 HGNC ID HGNC:8149 Link Image
Enzyme 2 Chromosome Location 8
Enzyme 2 Locus 8q24.3
Enzyme 2 SNPs SNPJam Report Link Image
Enzyme 2 General References Not Available
Enzyme 2 Metabolite References Not Available
Enzyme 3 [top]
Enzyme 3 ID 13042
Enzyme 3 Name 5-oxoprolinase
Enzyme 3 Synonyms
  1. ATP-hydrolysing
Enzyme 3 Gene Name OPLAH
Enzyme 3 Protein Sequence >5-oxoprolinase 
MGSPEGRFHFAIDRGGTFTDVFAQCPGGHVRVLKLLSEDPANYADAPTEGIRRILEQEAG
MLLPRDQPLDSSHIASIRMGTTVATNALLERKGERVALLVTRGFRDLLHIGTQARGDLFD
LAVPMPEVLYEEVLEVDERVVLHRGEAGTGTPVKGRTGDLLEVQQPVDLGALRGKLEGLL
SRGIRSLAVVLMHSYTWAQHEQQVGVLARELGFTHVSLSSEAMPMVRIVPRGHTACADAY
LTPAIQRYVQGFCRGFQGQLKDVQVLFMRSDGGLAPMDTFSGSSAVLSGPAGGVVGYSAT
TYQQEGGQPVIGFDMGGTSTDVSRYAGEFEHVFEASTAGVTLQAPQLDINTVAAGGGSRL
FFRSGLFVVGPESAGAHPGPACYRKGGPVTVTDANLVLGRLLPASFPCIFGPGENQPLSP
EASRKALEAVATEVNSFLTNGPCPASPLSLEEVAMGFVRVANEAMCRPIRALTQARGHDP
SAHVLACFGGAGGQHACAIARALGMDTVHIHRHSGLLSALGLALADVVHEAQEPCSLLYA
PETFVQLDQRLSRLEEQCVDALQAQGFPRSQISTESFLHLRYQGTDCALMVSAHQHPATA
RSPRAGDFGAAFVERYMREFGFVIPERPVVVDDVRVRGTGRSGLRLEDAPKAQTGPPRVD
KMTQCYFEGGYQETPVYLLAELGYGHKLHGPCLIIDSNSTILVEPGCQAEVTKTGDICIS
VGAEVPGTVGPQLDPIQLSIFSHRFMSIAEQMGRILQRTAISTNIKERLDFSCALFGPDG
GLVSNAPHIPVHLGAMQETVQFQIQHLGADLHPGDVLLSNHPSAGGSHLPDLTVITPVFW
PGQTRPVFYVASRGHHADIGGITPGSMPPHSTMLQQEGAVFLSFKLVQGGVFQEEAVTEA
LRAPGKVPNCSGTRNLHDNLSDLRAQVAANQKGIQLVGELIGQYGLDVVQAYMGHIQANA
ELAVRDMLRAFGTSRQARGLPLEVSSEDHMDDGSPIRLRVQISLSQGSAVFDFSGTGPEV
FGNLNAPRAVTLSALIYCLRCLVGRDIPLNQGCLAPVRVVIPRGSILDPSPEAAVVGGNV
LTSQRVVDVILGAFGACAASQGCMNNVTLGNAHMGYYETVAGGAGAGPSWHGRSGVHSHM
TNTRITDPEILESRYPVILRRFELRRGSGGRGRFRGGDGVTRELLFREEALLSVLTERRA
FRPYGLHGGEPGARGLNLLIRKNGRTVNLGGKTSVTVYPGDVFCLHTPGGGGYGDPEDPA
PPPGSPPQALAFPEHGSVYEYRRAQEAV
Enzyme 3 Number of Residues 1288
Enzyme 3 Molecular Weight 137459
Enzyme 3 Theoretical pI 6.56
Enzyme 3 GO Classification
Function
  • catalytic activity
  • hydrolase activity
Process
—
Component
—
Enzyme 3 General Function Amino acid transport and metabolism
Enzyme 3 Specific Function Not Available
Enzyme 3 Pathways Not Available
Enzyme 3 Reactions Not Available
Enzyme 3 Pfam Domain Function
Enzyme 3 Signals
  • None
Enzyme 3 Transmembrane Regions
  • None
Enzyme 3 Essentiality Not Available
Enzyme 3 GenBank ID Protein 148745653 Link Image
Enzyme 3 UniProtKB/Swiss-Prot ID A5PKY8 Link Image
Enzyme 3 UniProtKB/Swiss-Prot Entry Name A5PKY8_HUMAN Link Image
Enzyme 3 PDB ID Not Available
Enzyme 3 Cellular Location Not Available
Enzyme 3 Gene Sequence Not Available
Enzyme 3 GenBank Gene ID BC142672 Link Image
Enzyme 3 GeneCard ID A5PKY8 Link Image
Enzyme 3 GenAtlas ID Not Available
Enzyme 3 HGNC ID Not Available
Enzyme 3 Chromosome Location Not Available
Enzyme 3 Locus Not Available
Enzyme 3 SNPs SNPJam Report Link Image
Enzyme 3 General References
  1. Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA: Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proc Natl Acad Sci U S A. 2002 Dec 24;99(26):16899-903. Epub 2002 Dec 11. [PubMed Link Image]
Enzyme 3 Metabolite References Not Available
Enzyme 4 [top]
Enzyme 4 ID 15259
Enzyme 4 Name Gamma-glutamylcyclotransferase
Enzyme 4 Synonyms
  1. Cytochrome c-releasing factor 21
Enzyme 4 Gene Name GGCT
Enzyme 4 Protein Sequence >Gamma-glutamylcyclotransferase 
MANSGCKDVTGPDEESFLYFAYGSNLLTERIHLRNPSAAFFCVARLQDFKLDFGNSQGKT
SQTWHGGIATIFQSPGDEVWGVVWKMNKSNLNSLDEQEGVKSGMYVVIEVKVATQEGKEI
TCRSYLMTNYESAPPSPQYKKIICMGAKENGLPLEYQEKLKAIEPNDYTGKVSEEIEDII
KKGETQTL
Enzyme 4 Number of Residues 188
Enzyme 4 Molecular Weight 21008
Enzyme 4 Theoretical pI 4.79
Enzyme 4 GO Classification Not Available
Enzyme 4 General Function Not Available
Enzyme 4 Specific Function Catalyzes the formation of 5-oxoproline from gamma- glutamyl dipeptides and may play a significant role in glutathione homeostasis. Induces release of cytochrome c from mitochondria with resultant induction of apoptosis
Enzyme 4 Pathways Not Available
Enzyme 4 Reactions Not Available
Enzyme 4 Pfam Domain Function Not Available
Enzyme 4 Signals
  • None
Enzyme 4 Transmembrane Regions
  • None
Enzyme 4 Essentiality Not Available
Enzyme 4 GenBank ID Protein 189054993 Link Image
Enzyme 4 UniProtKB/Swiss-Prot ID O75223 Link Image
Enzyme 4 UniProtKB/Swiss-Prot Entry Name GGCT_HUMAN Link Image
Enzyme 4 PDB ID Not Available
Enzyme 4 Cellular Location Not Available
Enzyme 4 Gene Sequence >567 bp 
ATGGCCAACTCGGGCTGCAAGGACGTCACGGGTCCAGATGAGGAGAGTTTTCTGTACTTT
GCCTACGGCAGCAACCTGCTGACAGAGAGGATCCACCTCCGAAACCCCTCGGCGGCGTTC
TTCTGTGTGGCCCGCCTGCAGGATTTTAAGCTTGACTTTGGCAATTCCCAAGGCAAAACA
AGTCAAACTTGGCATGGAGGGATAGCCACCATTTTTCAGAGTCCTGGCGATGAAGTGTGG
GGAGTAGTATGGAAAATGAACAAAAGCAATTTAAATTCTCTGGATGAGCAAGAAGGGGTT
AAAAGTGGAATGTATGTTGTAATAGAAGTTAAAGTTGCAACTCAAGAAGGAAAAGAAATA
ACCTGTCGAAGTTATCTGATGACAAATTACGAAAGTGCTCCCCCATCCCCACAGTATAAA
AAGATTATTTGCATGGGTGCAAAAGAAAATGGTTTGCCGCTGGAGTATCAAGAGAAGTTA
AAAGCAATAGAACCAAATGACTATACAGGAAAGGTCTCAGAAGAAATTGAAGACATCATC
AAAAAGGGGGAAACACAAACTCTTTAG
Enzyme 4 GenBank Gene ID AK315608 Link Image
Enzyme 4 GeneCard ID O75223 Link Image
Enzyme 4 GenAtlas ID GGCT Link Image
Enzyme 4 HGNC ID HGNC:21705 Link Image
Enzyme 4 Chromosome Location Not Available
Enzyme 4 Locus Not Available
Enzyme 4 SNPs SNPJam Report Link Image
Enzyme 4 General References Not Available
Enzyme 4 Metabolite References Not Available