Glyoxylate metabolism and glycine degradation (Homo sapiens)

From WikiPathways

Revision as of 12:26, 18 November 2015 by ReactomeTeam (Talk | contribs)
(diff) ←Older revision | Current revision (diff) | Newer revision→ (diff)
Jump to: navigation, search
710, 234, 11-132, 186, 219, 205, 15, 191, 8, 14, 17, 2234, 11-13cytosolmitochondrial matrixperoxisomal matrixSAMDLL FAD H2OGCSH NH4+DLD AGXT dimerDAO NADP+FAD NADPHPYRAMTNAD+HAO1 tetramerDAO dimerglyoxylateAGXT2 tetramerglyoxylateGLDC O2FMN H2O2O2PXLP-AGXT2 PXLP-AGXT DLD dimer:2xFADGLDC dimer:2xPXLPH+L-AlaH+GCSH:SAMDLL5,10MTHFlipoyl-K107-GCSHHAO1 CO2NADHH2O2O2GCSH L-AlaTHFNH3H2ODHLL GRHPRGCSH:DHLLGlyPYRPXLP GlyGlycolateOX1717169


Description

Glyoxylate is generated in the course of glycine and hydroxyproline catabolism and can be converted to oxalate. In humans, this process takes place in the liver. Defects in two enzymes of glyoxylate metabolism, alanine:glyoxylate aminotransferase (AGXT) and glycerate dehydrogenase/glyoxylate reductase (GRHPR), are associated with pathogenic overproduction of oxalate (Danpure 2005). The reactions that interconvert glycine, glycolate, and glyoxylate and convert glyoxylate to oxalate have been characterized in molecular detail in humans. A reaction sequence for the conversion of hydroxyproline to glyoxylate has been inferred from studies of partially purified extracts of rat and bovine liver but the enzymes involved in the corresponding human reactions have not been identified. View original pathway at:Reactome.

Try the New WikiPathways

View approved pathways at the new wikipathways.org.

Quality Tags

Ontology Terms

 

Bibliography

View all...
  1. Brautigam CA, Chuang JL, Tomchick DR, Machius M, Chuang DT.; ''Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations.''; PubMed Europe PMC Scholia
  2. Morikawa T, Yasuno R, Wada H.; ''Do mammalian cells synthesize lipoic acid? Identification of a mouse cDNA encoding a lipoic acid synthase located in mitochondria.''; PubMed Europe PMC Scholia
  3. Kawazoe T, Tsuge H, Pilone MS, Fukui K.; ''Crystal structure of human D-amino acid oxidase: context-dependent variability of the backbone conformation of the VAAGL hydrophobic stretch located at the si-face of the flavin ring.''; PubMed Europe PMC Scholia
  4. Zhang X, Roe SM, Hou Y, Bartlam M, Rao Z, Pearl LH, Danpure CJ.; ''Crystal structure of alanine:glyoxylate aminotransferase and the relationship between genotype and enzymatic phenotype in primary hyperoxaluria type 1.''; PubMed Europe PMC Scholia
  5. Cramer SD, Ferree PM, Lin K, Milliner DS, Holmes RP.; ''The gene encoding hydroxypyruvate reductase (GRHPR) is mutated in patients with primary hyperoxaluria type II.''; PubMed Europe PMC Scholia
  6. Riedel TJ, Johnson LC, Knight J, Hantgan RR, Holmes RP, Lowther WT.; ''Structural and biochemical studies of human 4-hydroxy-2-oxoglutarate aldolase: implications for hydroxyproline metabolism in primary hyperoxaluria.''; PubMed Europe PMC Scholia
  7. Wynn RM, Kochi H, Cox RP, Chuang DT.; ''Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence.''; PubMed Europe PMC Scholia
  8. Srivastava D, Singh RK, Moxley MA, Henzl MT, Becker DF, Tanner JJ.; ''The three-dimensional structural basis of type II hyperprolinemia.''; PubMed Europe PMC Scholia
  9. Summitt CB, Johnson LC, Jönsson TJ, Parsonage D, Holmes RP, Lowther WT.; ''Proline dehydrogenase 2 (PRODH2) is a hydroxyproline dehydrogenase (HYPDH) and molecular target for treating primary hyperoxaluria.''; PubMed Europe PMC Scholia
  10. Fujiwara K, Okamura-Ikeda K, Motokawa Y.; ''Mechanism of the glycine cleavage reaction. Further characterization of the intermediate attached to H-protein and of the reaction catalyzed by T-protein.''; PubMed Europe PMC Scholia
  11. Tamaki N, Kaneko M, Mizota C, Kikugawa M, Fujimoto S.; ''Purification, characterization and inhibition of D-3-aminoisobutyrate aminotransferase from the rat liver.''; PubMed Europe PMC Scholia
  12. Moxley MA, Tanner JJ, Becker DF.; ''Steady-state kinetic mechanism of the proline:ubiquinone oxidoreductase activity of proline utilization A (PutA) from Escherichia coli.''; PubMed Europe PMC Scholia
  13. Williams E, Cregeen D, Rumsby G.; ''Identification and expression of a cDNA for human glycolate oxidase.''; PubMed Europe PMC Scholia
  14. Schonauer MS, Kastaniotis AJ, Kursu VA, Hiltunen JK, Dieckmann CL.; ''Lipoic acid synthesis and attachment in yeast mitochondria.''; PubMed Europe PMC Scholia
  15. Takada Y, Kaneko N, Esumi H, Purdue PE, Danpure CJ.; ''Human peroxisomal L-alanine: glyoxylate aminotransferase. Evolutionary loss of a mitochondrial targeting signal by point mutation of the initiation codon.''; PubMed Europe PMC Scholia
  16. Mayr JA, Zimmermann FA, Fauth C, Bergheim C, Meierhofer D, Radmayr D, Zschocke J, Koch J, Sperl W.; ''Lipoic acid synthetase deficiency causes neonatal-onset epilepsy, defective mitochondrial energy metabolism, and glycine elevation.''; PubMed Europe PMC Scholia
  17. Martini F, Angelaccio S, Barra D, Pascarella S, Maras B, Doonan S, Bossa F.; ''The primary structure of mitochondrial aspartate aminotransferase from human heart.''; PubMed Europe PMC Scholia
  18. Chang CF, Chou HT, Chuang JL, Chuang DT, Huang TH.; ''Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex.''; PubMed Europe PMC Scholia
  19. Katane M, Saitoh Y, Hanai T, Sekine M, Furuchi T, Koyama N, Nakagome I, Tomoda H, Hirono S, Homma H.; ''Thiolactomycin inhibits D-aspartate oxidase: a novel approach to probing the active site environment.''; PubMed Europe PMC Scholia
  20. Harris RA, Bowker-Kinley MM, Wu P, Jeng J, Popov KM.; ''Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex.''; PubMed Europe PMC Scholia
  21. Kume A, Koyata H, Sakakibara T, Ishiguro Y, Kure S, Hiraga K.; ''The glycine cleavage system. Molecular cloning of the chicken and human glycine decarboxylase cDNAs and some characteristics involved in the deduced protein structures.''; PubMed Europe PMC Scholia
  22. Fujiwara K, Okamura-Ikeda K, Motokawa Y.; ''Lipoylation of H-protein of the glycine cleavage system. The effect of site-directed mutagenesis of amino acid residues around the lipoyllysine residue on the lipoate attachment.''; PubMed Europe PMC Scholia
  23. Fujiwara K, Suzuki M, Okumachi Y, Okamura-Ikeda K, Fujiwara T, Takahashi E, Motokawa Y.; ''Molecular cloning, structural characterization and chromosomal localization of human lipoyltransferase gene.''; PubMed Europe PMC Scholia
  24. Danpure CJ, Jennings PR.; ''Further studies on the activity and subcellular distribution of alanine:glyoxylate aminotransferase in the livers of patients with primary hyperoxaluria type 1.''; PubMed Europe PMC Scholia
  25. Fujiwara K, Okamura-Ikeda K, Hayasaka K, Motokawa Y.; ''The primary structure of human H-protein of the glycine cleavage system deduced by cDNA cloning.''; PubMed Europe PMC Scholia
  26. Rodionov RN, Murry DJ, Vaulman SF, Stevens JW, Lentz SR.; ''Human alanine-glyoxylate aminotransferase 2 lowers asymmetric dimethylarginine and protects from inhibition of nitric oxide production.''; PubMed Europe PMC Scholia
  27. MAITRA U, DEKKER EE.; ''PURIFICATION AND PROPERTIES OF RAT LIVER 2-KETO-4-HYDROXYGLUTARATE ALDOLASE.''; PubMed Europe PMC Scholia
  28. Wanders RJ, Waterham HR, Ferdinandusse S.; ''Metabolic Interplay between Peroxisomes and Other Subcellular Organelles Including Mitochondria and the Endoplasmic Reticulum.''; PubMed Europe PMC Scholia
  29. Coulter-Mackie MB, Lian Q, Wong SG.; ''Overexpression of human alanine:glyoxylate aminotransferase in Escherichia coli: renaturation from guanidine-HCl and affinity for pyridoxal phosphate co-factor.''; PubMed Europe PMC Scholia
  30. MAITRA U, DEEKKER E.; ''PURIFICATION OF RAT-LIVER GAMMA-HYDROXYGLUTAMATE TRANSAMINASE AND ITS PROBABLE IDENTITY WITH GLUTAMATE-ASPARTATE TRANSAMINASE.''; PubMed Europe PMC Scholia
  31. Pakhomova S, Luka Z, Grohmann S, Wagner C, Newcomer ME.; ''Glycine N-methyltransferases: a comparison of the crystal structures and kinetic properties of recombinant human, mouse and rat enzymes.''; PubMed Europe PMC Scholia
  32. ADAMS E, GOLDSTONE A.; ''Hydroxyproline metabolism. IV. Enzymatic synthesis of gamma-hydroxyglutamate from Delta 1-pyrroline-3-hydroxy-5-carboxylate.''; PubMed Europe PMC Scholia
  33. Valle D, Goodman SI, Harris SC, Phang JM.; ''Genetic evidence for a common enzyme catalyzing the second step in the degradation of proline and hydroxyproline.''; PubMed Europe PMC Scholia
  34. Rokka A, Antonenkov VD, Soininen R, Immonen HL, Pirilä PL, Bergmann U, Sormunen RT, Weckström M, Benz R, Hiltunen JK.; ''Pxmp2 is a channel-forming protein in Mammalian peroxisomal membrane.''; PubMed Europe PMC Scholia
  35. Purdue PE, Takada Y, Danpure CJ.; ''Identification of mutations associated with peroxisome-to-mitochondrion mistargeting of alanine/glyoxylate aminotransferase in primary hyperoxaluria type 1.''; PubMed Europe PMC Scholia
  36. Danpure CJ.; ''Primary hyperoxaluria: from gene defects to designer drugs?''; PubMed Europe PMC Scholia
  37. Amery L, Brees C, Baes M, Setoyama C, Miura R, Mannaerts GP, Van Veldhoven PP.; ''C-terminal tripeptide Ser-Asn-Leu (SNL) of human D-aspartate oxidase is a functional peroxisome-targeting signal.''; PubMed Europe PMC Scholia
  38. Tort F, Ferrer-Cortès X, Thió M, Navarro-Sastre A, Matalonga L, Quintana E, Bujan N, Arias A, García-Villoria J, Acquaviva C, Vianey-Saban C, Artuch R, García-Cazorla À, Briones P, Ribes A.; ''Mutations in the lipoyltransferase LIPT1 gene cause a fatal disease associated with a specific lipoylation defect of the 2-ketoacid dehydrogenase complexes.''; PubMed Europe PMC Scholia
  39. Setoyama C, Miura R.; ''Structural and functional characterization of the human brain D-aspartate oxidase.''; PubMed Europe PMC Scholia
  40. Jones JM, Morrell JC, Gould SJ.; ''Identification and characterization of HAOX1, HAOX2, and HAOX3, three human peroxisomal 2-hydroxy acid oxidases.''; PubMed Europe PMC Scholia
  41. Adams E, Frank L.; ''Metabolism of proline and the hydroxyprolines.''; PubMed Europe PMC Scholia
  42. Vignaud C, Pietrancosta N, Williams EL, Rumsby G, Lederer F.; ''Purification and characterization of recombinant human liver glycolate oxidase.''; PubMed Europe PMC Scholia
  43. Brown RM, Head RA, Brown GK.; ''Pyruvate dehydrogenase E3 binding protein deficiency.''; PubMed Europe PMC Scholia
  44. Murray MS, Holmes RP, Lowther WT.; ''Active site and loop 4 movements within human glycolate oxidase: implications for substrate specificity and drug design.''; PubMed Europe PMC Scholia
  45. Molla G, Sacchi S, Bernasconi M, Pilone MS, Fukui K, Polegioni L.; ''Characterization of human D-amino acid oxidase.''; PubMed Europe PMC Scholia
  46. Forte-McRobbie CM, Pietruszko R.; ''Purification and characterization of human liver "high Km" aldehyde dehydrogenase and its identification as glutamic gamma-semialdehyde dehydrogenase.''; PubMed Europe PMC Scholia
  47. Rumsby G, Cregeen DP.; ''Identification and expression of a cDNA for human hydroxypyruvate/glyoxylate reductase.''; PubMed Europe PMC Scholia
  48. Da Cruz S, Xenarios I, Langridge J, Vilbois F, Parone PA, Martinou JC.; ''Proteomic analysis of the mouse liver mitochondrial inner membrane.''; PubMed Europe PMC Scholia
  49. Atlante A, Seccia TM, Marra E, Minervini GM, Vulpis V, Pirrelli A, Passarella S.; ''Carrier-mediated transport controls hydroxyproline catabolism in heart mitochondria from spontaneously hypertensive rat.''; PubMed Europe PMC Scholia
  50. Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chrétien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P.; ''Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.''; PubMed Europe PMC Scholia
  51. Ciszak EM, Makal A, Hong YS, Vettaikkorumakankauv AK, Korotchkina LG, Patel MS.; ''How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex.''; PubMed Europe PMC Scholia
  52. Katane M, Kawata T, Nakayama K, Saitoh Y, Kaneko Y, Matsuda S, Saitoh Y, Miyamoto T, Sekine M, Homma H.; ''Characterization of the enzymatic and structural properties of human D-aspartate oxidase and comparison with those of the rat and mouse enzymes.''; PubMed Europe PMC Scholia
  53. Negri A, Ceciliani F, Tedeschi G, Simonic T, Ronchi S.; ''The primary structure of the flavoprotein D-aspartate oxidase from beef kidney.''; PubMed Europe PMC Scholia
  54. ADAMS E, GOLDSTONE A.; ''Hydroxyproline metabolism. II. Enzymatic preparation and properties of Delta 1-pyrroline-3-hydroxy-5-carboxylic acid.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
114656view16:12, 25 January 2021ReactomeTeamReactome version 75
113104view11:16, 2 November 2020ReactomeTeamReactome version 74
112338view15:26, 9 October 2020ReactomeTeamReactome version 73
101238view11:13, 1 November 2018ReactomeTeamreactome version 66
100777view20:40, 31 October 2018ReactomeTeamreactome version 65
100320view19:17, 31 October 2018ReactomeTeamreactome version 64
99865view16:00, 31 October 2018ReactomeTeamreactome version 63
99422view14:36, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99105view12:39, 31 October 2018ReactomeTeamreactome version 62
93997view13:50, 16 August 2017ReactomeTeamreactome version 61
93606view11:28, 9 August 2017ReactomeTeamreactome version 61
87455view14:02, 22 July 2016MkutmonOntology Term : 'glyoxylate and dicarboxylate metabolic pathway' added !
86713view09:24, 11 July 2016ReactomeTeamreactome version 56
83452view12:26, 18 November 2015ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
5,10MTHFMetaboliteCHEBI:12071 (ChEBI)
AGXT dimerComplexR-HSA-389671 (Reactome)
AGXT2 tetramerComplexR-HSA-904854 (Reactome)
AMTProteinP48728 (Uniprot-TrEMBL)
CO2MetaboliteCHEBI:16526 (ChEBI)
DAO ProteinP14920 (Uniprot-TrEMBL)
DAO dimerComplexR-HSA-389849 (Reactome)
DHLL MetaboliteCHEBI:50746 (ChEBI)
DLD ProteinP09622 (Uniprot-TrEMBL)
DLD dimer:2xFADComplexR-HSA-5694020 (Reactome)
FAD MetaboliteCHEBI:16238 (ChEBI)
FMN MetaboliteCHEBI:17621 (ChEBI)
GCSH ProteinP23434 (Uniprot-TrEMBL)
GCSH:DHLLComplexR-HSA-5693982 (Reactome)
GCSH:SAMDLLComplexR-HSA-5693969 (Reactome)
GLDC ProteinP23378 (Uniprot-TrEMBL)
GLDC dimer:2xPXLPComplexR-HSA-5693954 (Reactome)
GRHPRProteinQ9UBQ7 (Uniprot-TrEMBL)
GlyMetaboliteCHEBI:15428 (ChEBI)
GlycolateMetaboliteCHEBI:17497 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
H2O2MetaboliteCHEBI:16240 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HAO1 ProteinQ9UJM8 (Uniprot-TrEMBL)
HAO1 tetramerComplexR-HSA-389845 (Reactome)
L-AlaMetaboliteCHEBI:16977 (ChEBI)
NAD+MetaboliteCHEBI:15846 (ChEBI)
NADHMetaboliteCHEBI:16908 (ChEBI)
NADP+MetaboliteCHEBI:18009 (ChEBI)
NADPHMetaboliteCHEBI:16474 (ChEBI)
NH3MetaboliteCHEBI:16134 (ChEBI)
NH4+MetaboliteCHEBI:28938 (ChEBI)
O2MetaboliteCHEBI:15379 (ChEBI)
OXMetaboliteCHEBI:16995 (ChEBI)
PXLP MetaboliteCHEBI:18405 (ChEBI)
PXLP-AGXT ProteinP21549 (Uniprot-TrEMBL)
PXLP-AGXT2 ProteinQ9BYV1 (Uniprot-TrEMBL)
PYRMetaboliteCHEBI:32816 (ChEBI)
SAMDLL MetaboliteCHEBI:14949 (ChEBI)
THFMetaboliteCHEBI:15635 (ChEBI)
glyoxylateMetaboliteCHEBI:16891 (ChEBI)
lipoyl-K107-GCSHProteinP23434 (Uniprot-TrEMBL)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
5,10MTHFArrowR-HSA-5693977 (Reactome)
AGXT dimermim-catalysisR-HSA-389684 (Reactome)
AGXT2 tetramermim-catalysisR-HSA-904864 (Reactome)
AMTmim-catalysisR-HSA-5693977 (Reactome)
CO2ArrowR-HSA-5693967 (Reactome)
DAO dimermim-catalysisR-HSA-389821 (Reactome)
DLD dimer:2xFADmim-catalysisR-HSA-5694018 (Reactome)
GCSH:DHLLArrowR-HSA-5693977 (Reactome)
GCSH:DHLLR-HSA-5694018 (Reactome)
GCSH:SAMDLLArrowR-HSA-5693967 (Reactome)
GCSH:SAMDLLR-HSA-5693977 (Reactome)
GLDC dimer:2xPXLPmim-catalysisR-HSA-5693967 (Reactome)
GRHPRmim-catalysisR-HSA-389826 (Reactome)
GlyArrowR-HSA-389684 (Reactome)
GlyArrowR-HSA-904864 (Reactome)
GlyR-HSA-389821 (Reactome)
GlyR-HSA-5693967 (Reactome)
GlycolateArrowR-HSA-389826 (Reactome)
GlycolateR-HSA-389842 (Reactome)
H+ArrowR-HSA-5694018 (Reactome)
H+R-HSA-389826 (Reactome)
H2O2ArrowR-HSA-389821 (Reactome)
H2O2ArrowR-HSA-389842 (Reactome)
H2O2ArrowR-HSA-389862 (Reactome)
H2OR-HSA-389821 (Reactome)
H2OR-HSA-389862 (Reactome)
HAO1 tetramermim-catalysisR-HSA-389842 (Reactome)
HAO1 tetramermim-catalysisR-HSA-389862 (Reactome)
L-AlaR-HSA-389684 (Reactome)
L-AlaR-HSA-904864 (Reactome)
NAD+R-HSA-5694018 (Reactome)
NADHArrowR-HSA-5694018 (Reactome)
NADP+ArrowR-HSA-389826 (Reactome)
NADPHR-HSA-389826 (Reactome)
NH3ArrowR-HSA-5693977 (Reactome)
NH4+ArrowR-HSA-389821 (Reactome)
O2R-HSA-389821 (Reactome)
O2R-HSA-389842 (Reactome)
O2R-HSA-389862 (Reactome)
OXArrowR-HSA-389862 (Reactome)
PYRArrowR-HSA-389684 (Reactome)
PYRArrowR-HSA-904864 (Reactome)
R-HSA-389684 (Reactome) Alanine-glyoxylate transaminase (AGXT) catalyzes the irreversible reaction of glyoxylate and alanine to form glycine and pyruvate (Danpure and Jennings 1988). The active form of the enzyme is a homodimer (Zhang et al. 2003) with one molecule of pyridoxal phosphate bound to each subunit (Coulter-Mackie et al. 2005). Mutations in this enzyme are associated with primary hyperoxaluria type I. Mutant alleles encode both catalytically inactive proteins and active ones that are mis-localized to mitochondria (Purdue et al. 1990; Takada et al. 1990).
R-HSA-389821 (Reactome) Peroxisomal D-amino-acid oxidase catalyzes the reaction of glycine, water, and O2 to form glyoxylate, H2O2, and NH4+. The active form of the enzyme is a homodimer and has FAD as a cofactor (Kawazoe et al. 2006; Molla et al. 2006).
R-HSA-389826 (Reactome) Peroxisomal GRHPR catalyzes the reaction of glyoxylate and NADPH + H+ to form glycolate and NADP+. The active form of the enzyme is a monomer (Rumsby and Cregeen 1999); mutations in it are associated with primary hyperoxaluria type II (Cramer et al. 1999).
R-HSA-389842 (Reactome) Peroxisomal hydroxyacid oxidase 1 catalyzes the reaction of glycolate and O2 to form glyoxylate and H2O2. The active form of the enzyme is associated with FMN and is a tetramer (Jones et al. 2000; Murray et al. 2008; Vignaud et al. 2007; Williams et al. 2000).
R-HSA-389862 (Reactome) Peroxisomal hydroxyacid oxidase 1 catalyzes the reaction of glyoxylate to form oxalate. The active form of the enzyme is associated with FMN and is a tetramer (Jones et al. 2000; Murray et al. 2008; Vignaud et al. 2007; Williams et al. 2000).
R-HSA-5693967 (Reactome) The simplest amino acid, glycine, is catabolised by several different pathways. The major pathway is via the glycine cleavage system. In the first reaction, glycine (Gly) is decarboxylated to carbon dioxide (CO2) and aminomethyl group (NH2CH2) by mitochondrial glycine dehydrogenase (decarboxylating) (GLDC, P protein), a dimeric protein using pyridoxal 5-phosphate (PXPL) as cofactor per subunit (Kume et al. 1991). Mitochondrial glycine cleavage system H protein (GCSH) is used as a co-substrate in this reaction. GCSH uses lipoate as a cofactor which accepts the aminomethylgroup from glycine decarboxylation to form a S-aminomethyldihydrolipoylated protein (GCSH:SAMDLL) (Fujiwara et al. 1991, Fujiwara et al. 1991).
R-HSA-5693977 (Reactome) The major degradative pathway for the amino acid glycine is via the glycine cleavage system. In the second reaction in this system, the decarboxylated moiety from glycine decarboxylation attached to H protein (GCSH:SAMDLL) is further degraded by mitochondrial aminomethyltransferase (AMT, GCST, T protein) to ammonia (NH3) and GCSH with reduced lipoate. Tetrahydrofolate (THF) is required for this reaction and accepts the methyl group to form 5,10MTHF (Fujiwara et al. 1984).
R-HSA-5694018 (Reactome) The last step in the glycine cleavage system is the reoxidation of the reduced lipoate (dihydrolipoyl group) attached to the H protein (GCSH:DHLL) catalysed by the L protein (mitochondrial dihydrolipoyl dehydrogenase, DLD) (Harris et al. 1997, Ciszak et al. 2006).
R-HSA-904864 (Reactome) Mitochondrial AGXT2 (alanine-glyoxylate transaminase 2) catalyzes the irreversible reaction of glyoxylate and alanine to form glycine and pyruvate (Rodionov et al. 2010). The active form of the enzyme is inferred to be a homotetramer from the properties of the homologous rat protein, which has been purified and characterized in vitro (Tamaki et al.990). Most conversion of glyoxylate to glycine in vivo appears to occur in the peroxisome, catalyzed by AGXT, and the physiological role of the AGXT2 reaction is unclear.
THFR-HSA-5693977 (Reactome)
glyoxylateArrowR-HSA-389821 (Reactome)
glyoxylateArrowR-HSA-389842 (Reactome)
glyoxylateR-HSA-389684 (Reactome)
glyoxylateR-HSA-389826 (Reactome)
glyoxylateR-HSA-389862 (Reactome)
glyoxylateR-HSA-904864 (Reactome)
lipoyl-K107-GCSHArrowR-HSA-5694018 (Reactome)
lipoyl-K107-GCSHR-HSA-5693967 (Reactome)
Retrieved from "https://classic.wikipathways.org/index.php/Pathway:WP3562"
Personal tools