Record Information
Version 1.0
Update Date 1/22/2018 12:54:54 PM
Metabolite IDPAMDB000046
Identification
Name: Glycine
Description:Glycine is a simple amino acid. The glycine cleavage enzyme system comprises four proteins: P-, T-, H- and L-proteins (EC 1.4.4.2, EC 2.1.2.10 and EC 1.8.1.4 for P-, T- and L-proteins). The glycine cleavage system catalyses the oxidative conversion of glycine into carbon dioxide and ammonia, with the remaining one-carbon unit transferred to folate as methylenetetrahydrofolate. It is the main catabolic pathway for glycine and it also contributes to one-carbon metabolism.
Structure
Thumb
Synonyms:
  • 2-Aminoacetate
  • 2-Aminoacetic acid
  • Aciport
  • Amino-Acetate
  • Amino-Acetic acid
  • Aminoacetate
  • Aminoacetic acid
  • Aminoethanoate
  • Aminoethanoic acid
  • G
  • Glicoamin
  • Gly
  • Glycocoll
  • Glycolixir
  • Glycosthene
  • Gyn-Hydralin
  • Padil
Chemical Formula: C2H5NO2
Average Molecular Weight: 75.0666
Monoisotopic Molecular Weight: 75.032028409
InChI Key: DHMQDGOQFOQNFH-UHFFFAOYSA-N
InChI:InChI=1S/C2H5NO2/c3-1-2(4)5/h1,3H2,(H,4,5)
CAS number: 56-40-6
IUPAC Name:2-aminoacetic acid
Traditional IUPAC Name: glycine
SMILES:NCC(O)=O
Chemical Taxonomy
Taxonomy DescriptionThis compound belongs to the class of organic compounds known as alpha amino acids. These are amino acids in which the amino group is attached to the carbon atom immediately adjacent to the carboxylate group (alpha carbon).
Kingdom Organic compounds
Super ClassOrganic acids and derivatives
Class Carboxylic acids and derivatives
Sub ClassAmino acids, peptides, and analogues
Direct Parent Alpha amino acids
Alternative Parents
Substituents
  • Alpha-amino acid
  • Monocarboxylic acid or derivatives
  • Carboxylic acid
  • Hydrocarbon derivative
  • Primary amine
  • Organooxygen compound
  • Organonitrogen compound
  • Primary aliphatic amine
  • Carbonyl group
  • Amine
  • Aliphatic acyclic compound
Molecular Framework Aliphatic acyclic compounds
External Descriptors
Physical Properties
State: Solid
Charge:0
Melting point: 504 deg F
Experimental Properties:
PropertyValueSource
Water Solubility:249.0 mg/mL [YALKOWSKY,SH & DANNENFELSER,RM (1992)]PhysProp
LogP:-3.21 [HANSCH,C ET AL. (1995)]PhysProp
Predicted Properties
PropertyValueSource
Water Solubility552.0 mg/mLALOGPS
logP-3.3ALOGPS
logP-3.4ChemAxon
logS0.87ALOGPS
pKa (Strongest Acidic)2.31ChemAxon
pKa (Strongest Basic)9.24ChemAxon
Physiological Charge0ChemAxon
Hydrogen Acceptor Count3ChemAxon
Hydrogen Donor Count2ChemAxon
Polar Surface Area63.32 Å2ChemAxon
Rotatable Bond Count1ChemAxon
Refractivity16 m3·mol-1ChemAxon
Polarizability6.65 Å3ChemAxon
Number of Rings0ChemAxon
Bioavailability1ChemAxon
Rule of FiveYesChemAxon
Ghose FilterYesChemAxon
Veber's RuleYesChemAxon
MDDR-like RuleYesChemAxon
Biological Properties
Cellular Locations: Cytoplasm
Reactions:
Cysteinylglycine + Water > L-Cysteine + Glycine
L-Threonine <> Acetaldehyde + Glycine
L-Allothreonine > Acetaldehyde + Glycine
Glycine + NAD + Tetrahydrofolic acid > Carbon dioxide + 5,10-Methylene-THF + NADH + Ammonium
Adenosine triphosphate + Glycine + tRNA(Gly) + tRNA(Gly) <> Adenosine monophosphate + Glycyl-tRNA(Gly) + Pyrophosphate + Glycyl-tRNA(Gly)
Water + L-Prolinylglycine > Glycine + L-Proline
Water + Oxygen + Sarcosine > Formaldehyde + Glycine + Hydrogen peroxide
L-Serine + Tetrahydrofolic acid <> Glycine + Water + 5,10-Methylene-THF
Adenosine triphosphate + gamma-Glutamylcysteine + Glycine <> ADP + Glutathione + Hydrogen ion + Phosphate
Acetyl-CoA + Glycine <> L-2-Amino-3-oxobutanoic acid + Coenzyme A
Adenosine triphosphate + Glycine + 5-Phosphoribosylamine <> ADP + Glycineamideribotide + Hydrogen ion + Phosphate
Adenosine triphosphate + gamma-Glutamylcysteine + Glycine <> ADP + Phosphate + Glutathione
Glycine + Tetrahydrofolic acid + NAD <> 5,10-Methylene-THF + Ammonia + Carbon dioxide + NADH + Hydrogen ion
Glycine + Lipoylprotein <> S-Aminomethyldihydrolipoylprotein + Carbon dioxide
Adenosine triphosphate + Glycine + tRNA(Gly) <> Adenosine monophosphate + Pyrophosphate + Glycyl-tRNA(Gly)
Adenosine triphosphate + 5-Phosphoribosylamine + Glycine <> ADP + Phosphate + Glycineamideribotide
R-S-Cysteinylglycine + Water <> S-Substituted L-cysteine + Glycine
L-Serine + 5,6,7,8-Tetrahydromethanopterin <> 5,10-Methylenetetrahydromethanopterin + Glycine + Water
Glycine + Acetyl-CoA <> Hydrogen ion + L-2-Amino-3-oxobutanoic acid + Coenzyme A

Pathways:
Spectra
Spectra:
Spectrum TypeDescriptionSplash Key
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (3 TMS)splash10-00dj-2900000000-0ef96bcf06ce475afcddView in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies)splash10-00dj-1900000000-1d289099ac79cfb8bb19View in MoNA
GC-MSGC-MS Spectrum - GC-EI-TOF (Pegasus III TOF-MS system, Leco; GC 6890, Agilent Technologies) (3 TMS)splash10-00di-7910000000-6c972a683dfb75b69331View in MoNA
GC-MSGC-MS Spectrum - GC-MS (2 TMS)splash10-0udi-0900000000-ef69e38ee6cebc2ece00View in MoNA
GC-MSGC-MS Spectrum - GC-MS (3 TMS)splash10-00di-2910000000-3215b9e40f20c7b306cdView in MoNA
GC-MSGC-MS Spectrum - GC-MSNot Available
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 10V, Positive (Annotated)splash10-003r-9000000000-725357e461c898a7451eView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 25V, Positive (Annotated)splash10-001i-9000000000-9f3930e66b117ad91dcaView in MoNA
LC-MS/MSLC-MS/MS Spectrum - Quattro_QQQ 40V, Positive (Annotated)splash10-001i-9000000000-b3336097dddbb5e22871View in MoNA
LC-MS/MSLC-MS/MS Spectrum - EI-B (HITACHI RMU-6M) , Positivesplash10-001i-9000000000-719b7f248956f13a312dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, Negativesplash10-00di-9000000000-6001578fc511ba3fefefView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, Negativesplash10-00di-9000000000-79b2a0a9d93de6a62358View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, Negativesplash10-00di-9000000000-9290dbe208c4744f4431View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 10V, Positivesplash10-004i-9000000000-342ab462db0835abb3d2View in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 20V, Positivesplash10-0ar1-9010000000-9daadc1d169a8530926dView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 30V, Positivesplash10-07y0-9220000000-8c7785f1f3aa8052679fView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 40V, Positivesplash10-0ula-9110000000-43ada06fe1b56b4e9fccView in MoNA
LC-MS/MSLC-MS/MS Spectrum - LC-ESI-QQ (API3000, Applied Biosystems) 50V, Positivesplash10-017i-9000000000-fbd78fbb48f082235f42View in MoNA
LC-MS/MSLC-MS/MS Spectrum - CE-ESI-TOF (CE-system connected to 6210 Time-of-Flight MS, Agilent) , Positivesplash10-004i-9000000000-c38d0fb28793438083a9View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Positivesplash10-0059-9000000000-c6b1ebc1dba89b6a6184View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Positivesplash10-001i-9000000000-851aa6a0263541a8b249View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Positivesplash10-053r-9000000000-d3b5624412082bb2cf60View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 10V, Negativesplash10-00di-9000000000-89b2c043a5afe3ebc6f6View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 20V, Negativesplash10-00di-9000000000-b4046e208ee8adb87021View in MoNA
Predicted LC-MS/MSPredicted LC-MS/MS Spectrum - 40V, Negativesplash10-05fr-9000000000-36521e440c602bd2ca5aView in MoNA
MSMass Spectrum (Electron Ionization)splash10-001i-9000000000-222d6c3a1ba6afcd7ea9View in MoNA
1D NMR1H NMR SpectrumNot Available
1D NMR13C NMR SpectrumNot Available
1D NMR1H NMR SpectrumNot Available
1D NMR13C NMR SpectrumNot Available
1D NMR1H NMR SpectrumNot Available
2D NMR[1H,1H] 2D NMR SpectrumNot Available
2D NMR[1H,13C] 2D NMR SpectrumNot Available
References
References:
  • Bales JR, Higham DP, Howe I, Nicholson JK, Sadler PJ: Use of high-resolution proton nuclear magnetic resonance spectroscopy for rapid multi-component analysis of urine. Clin Chem. 1984 Mar;30(3):426-32. Pubmed: 6321058
  • Bennett FI, Jackson AA: Glycine is not formed through the amino transferase reaction in human or rat placenta. Placenta. 1998 May;19(4):329-31. Pubmed: 9639330
  • Boneh A, Degani Y, Harari M: Prognostic clues and outcome of early treatment of nonketotic hyperglycinemia. Pediatr Neurol. 1996 Sep;15(2):137-41. Pubmed: 8888048
  • Byard RW, Harrison R, Wells R, Gilbert JD: Glycine toxicity and unexpected intra-operative death. J Forensic Sci. 2001 Sep;46(5):1244-6. Pubmed: 11569574
  • Christie GR, Ford D, Howard A, Clark MA, Hirst BH: Glycine supply to human enterocytes mediated by high-affinity basolateral GLYT1. Gastroenterology. 2001 Feb;120(2):439-48. Pubmed: 11159884
  • Collins JW, Macdermott S, Bradbrook RA, Keeley FX Jr, Timoney AG: Is using ethanol-glycine irrigating fluid monitoring and 'good surgical practice' enough to prevent harmful absorption during transurethral resection of the prostate? BJU Int. 2006 Jun;97(6):1247-51. Pubmed: 16686720
  • 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
  • Dicke JM, Verges D, Kelley LK, Smith CH: Glycine uptake by microvillous and basal plasma membrane vesicles from term human placentae. Placenta. 1993 Jan-Feb;14(1):85-92. Pubmed: 8456092
  • 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
  • Gomeza J, Ohno K, Hulsmann S, Armsen W, Eulenburg V, Richter DW, Laube B, Betz H: Deletion of the mouse glycine transporter 2 results in a hyperekplexia phenotype and postnatal lethality. Neuron. 2003 Nov 13;40(4):797-806. Pubmed: 14622583
  • 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
  • Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597. Pubmed: 17379776
  • Jones CM, Smith M, Henderson MJ: Reference data for cerebrospinal fluid and the utility of amino acid measurement for the diagnosis of inborn errors of metabolism. Ann Clin Biochem. 2006 Jan;43(Pt 1):63-6. Pubmed: 16390611
  • Kanehisa, M., Goto, S., Sato, Y., Furumichi, M., Tanabe, M. (2012). "KEGG for integration and interpretation of large-scale molecular data sets." Nucleic Acids Res 40:D109-D114. Pubmed: 22080510
  • Keseler, I. M., Collado-Vides, J., Santos-Zavaleta, A., Peralta-Gil, M., Gama-Castro, S., Muniz-Rascado, L., Bonavides-Martinez, C., Paley, S., Krummenacker, M., Altman, T., Kaipa, P., Spaulding, A., Pacheco, J., Latendresse, M., Fulcher, C., Sarker, M., Shearer, A. G., Mackie, A., Paulsen, I., Gunsalus, R. P., Karp, P. D. (2011). "EcoCyc: a comprehensive database of Escherichia coli biology." Nucleic Acids Res 39:D583-D590. Pubmed: 21097882
  • Khan SA, Cox IJ, Hamilton G, Thomas HC, Taylor-Robinson SD: In vivo and in vitro nuclear magnetic resonance spectroscopy as a tool for investigating hepatobiliary disease: a review of H and P MRS applications. Liver Int. 2005 Apr;25(2):273-81. Pubmed: 15780050
  • 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
  • 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
  • Prescot AP, de B Frederick B, Wang L, Brown J, Jensen JE, Kaufman MJ, Renshaw PF: In vivo detection of brain glycine with echo-time-averaged (1)H magnetic resonance spectroscopy at 4.0 T. Magn Reson Med. 2006 Mar;55(3):681-6. Pubmed: 16453318
  • 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
  • Shoemaker JD, Elliott WH: Automated screening of urine samples for carbohydrates, organic and amino acids after treatment with urease. J Chromatogr. 1991 Jan 2;562(1-2):125-38. Pubmed: 2026685
  • Silwood CJ, Lynch E, Claxson AW, Grootveld MC: 1H and (13)C NMR spectroscopic analysis of human saliva. J Dent Res. 2002 Jun;81(6):422-7. Pubmed: 12097436
  • 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
  • van der Werf, M. J., Overkamp, K. M., Muilwijk, B., Coulier, L., Hankemeier, T. (2007). "Microbial metabolomics: toward a platform with full metabolome coverage." Anal Biochem 370:17-25. Pubmed: 17765195
  • Van Hove JL, Vande Kerckhove K, Hennermann JB, Mahieu V, Declercq P, Mertens S, De Becker M, Kishnani PS, Jaeken J: Benzoate treatment and the glycine index in nonketotic hyperglycinaemia. J Inherit Metab Dis. 2005;28(5):651-63. Pubmed: 16151895
  • Vijayendran, C., Barsch, A., Friehs, K., Niehaus, K., Becker, A., Flaschel, E. (2008). "Perceiving molecular evolution processes in Escherichia coli by comprehensive metabolite and gene expression profiling." Genome Biol 9:R72. Pubmed: 18402659
  • Winder, C. L., Dunn, W. B., Schuler, S., Broadhurst, D., Jarvis, R., Stephens, G. M., Goodacre, R. (2008). "Global metabolic profiling of Escherichia coli cultures: an evaluation of methods for quenching and extraction of intracellular metabolites." Anal Chem 80:2939-2948. Pubmed: 18331064
Synthesis Reference: Anslow, Winston K.; King, Harold. Synthesis of glycine. Journal of the Chemical Society (1929), 2163-6.
Material Safety Data Sheet (MSDS) Download (PDF)
External Links:
ResourceLink
CHEBI ID15428
HMDB IDHMDB00123
Pubchem Compound ID750
Kegg IDC00037
ChemSpider ID730
WikipediaGlycine
BioCyc IDGLY
EcoCyc IDGLY
Ligand ExpoGLY_LFZW

Enzymes

General function:
Involved in nucleotide binding
Specific function:
ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
Gene Name:
glyQ
Locus Tag:
PA0009
Molecular weight:
36.1 kDa
Reactions
ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).
General function:
Involved in arginine-tRNA ligase activity
Specific function:
ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly)
Gene Name:
glyS
Locus Tag:
PA0008
Molecular weight:
74 kDa
Reactions
ATP + glycine + tRNA(Gly) = AMP + diphosphate + glycyl-tRNA(Gly).
General function:
Involved in ATP binding
Specific function:
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione
Gene Name:
gshB
Locus Tag:
PA0407
Molecular weight:
35.7 kDa
Reactions
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.
General function:
Involved in proteolysis
Specific function:
Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation
Gene Name:
pepN
Locus Tag:
PA3083
Molecular weight:
100 kDa
Reactions
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
General function:
Involved in catalytic activity
Specific function:
Interconversion of serine and glycine
Gene Name:
glyA
Locus Tag:
PA4602
Molecular weight:
45.2 kDa
Reactions
5,10-methylenetetrahydrofolate + glycine + H(2)O = tetrahydrofolate + L-serine.
General function:
Involved in ATP binding
Specific function:
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide
Gene Name:
purD
Locus Tag:
PA4855
Molecular weight:
45.2 kDa
Reactions
ATP + 5-phospho-D-ribosylamine + glycine = ADP + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide.
General function:
Involved in aminomethyltransferase activity
Specific function:
The glycine cleavage system catalyzes the degradation of glycine
Gene Name:
gcvT
Locus Tag:
PA5215
Molecular weight:
38.9 kDa
Reactions
[Protein]-S(8)-aminomethyldihydrolipoyllysine + tetrahydrofolate = [protein]-dihydrolipoyllysine + 5,10-methylenetetrahydrofolate + NH(3).
General function:
Involved in glycine dehydrogenase (decarboxylating) activity
Specific function:
The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein
Gene Name:
gcvP
Locus Tag:
PA5213
Molecular weight:
104.7 kDa
Reactions
Glycine + H-protein-lipoyllysine = H-protein-S-aminomethyldihydrolipoyllysine + CO(2).
General function:
Involved in aminopeptidase activity
Specific function:
Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides. Required for plasmid ColE1 site-specific recombination but not in its aminopeptidase activity. Could act as a structural component of the putative nucleoprotein complex in which the Xer recombination reaction takes place
Gene Name:
pepA
Locus Tag:
PA3831
Molecular weight:
52.3 kDa
Reactions
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
General function:
Involved in lyase activity
Specific function:
Catalyzes the cleavage of L-allo-threonine and L- threonine to glycine and acetaldehyde. L-threo-phenylserine and L- erythro-phenylserine are also good substrates
Gene Name:
ltaE
Locus Tag:
PA0902
Molecular weight:
35.4 kDa
Reactions
L-threonine = glycine + acetaldehyde.
L-allo-threonine = glycine + acetaldehyde.
General function:
Amino acid transport and metabolism
Specific function:
The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein
Gene Name:
gcvH
Locus Tag:
PA5214
Molecular weight:
13.6 kDa

Transporters

General function:
Involved in proteolysis
Specific function:
Aminopeptidase N is involved in the degradation of intracellular peptides generated by protein breakdown during normal growth as well as in response to nutrient starvation
Gene Name:
pepN
Locus Tag:
PA3083
Molecular weight:
100 kDa
Reactions
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
General function:
Involved in sodium:amino acid symporter activity
Specific function:
Specific function unknown
Gene Name:
yaaJ
Locus Tag:
PA3641
Molecular weight:
50.3 kDa
General function:
Involved in nucleotide binding
Specific function:
Probably part of a binding-protein-dependent transport system yecCS for an amino acid. Probably responsible for energy coupling to the transport system
Gene Name:
yecC
Locus Tag:
PA5152
Molecular weight:
28.4 kDa