KEGG   PATHWAY: pvu00785
Entry
pvu00785                    Pathway                                
Name
Lipoic acid metabolism - Phaseolus vulgaris (common bean)
Class
Metabolism; Metabolism of cofactors and vitamins
Pathway map
pvu00785  Lipoic acid metabolism
pvu00785

Module
pvu_M00307  Pyruvate oxidation, pyruvate => acetyl-CoA [PATH:pvu00785]
pvu_M00621  Glycine cleavage system [PATH:pvu00785]
pvu_M00881  Lipoic acid biosynthesis, plants and bacteria, octanoyl-ACP => dihydrolipoyl-E2/H [PATH:pvu00785]
pvu_M00882  Lipoic acid biosynthesis, eukaryotes, octanoyl-ACP => dihydrolipoyl-H [PATH:pvu00785]
Other DBs
GO: 0009106
Organism
Phaseolus vulgaris (common bean) [GN:pvu]
Gene
PHAVU_005G120000g  hypothetical protein [KO:K03801] [EC:2.3.1.181]
PHAVU_006G040300g  hypothetical protein [KO:K03801] [EC:2.3.1.181]
PHAVU_002G015200g  hypothetical protein [KO:K23735] [EC:2.3.1.181]
PHAVU_007G045700g  hypothetical protein [KO:K23735] [EC:2.3.1.181]
PHAVU_007G046000g  hypothetical protein [KO:K23735] [EC:2.3.1.181]
PHAVU_005G072800g  hypothetical protein [KO:K03644] [EC:2.8.1.8]
PHAVU_007G021800g  hypothetical protein [KO:K03644] [EC:2.8.1.8]
PHAVU_005G106700g  hypothetical protein [KO:K03644] [EC:2.8.1.8]
PHAVU_003G112300g  hypothetical protein [KO:K00382] [EC:1.8.1.4]
PHAVU_003G118800g  hypothetical protein [KO:K00382] [EC:1.8.1.4]
PHAVU_009G254900g  hypothetical protein [KO:K00382] [EC:1.8.1.4]
PHAVU_009G257800g  hypothetical protein [KO:K00161] [EC:1.2.4.1]
PHAVU_010G119600g  hypothetical protein [KO:K00161] [EC:1.2.4.1]
PHAVU_002G077600g  hypothetical protein [KO:K00161] [EC:1.2.4.1]
PHAVU_003G056300g  hypothetical protein [KO:K00161] [EC:1.2.4.1]
PHAVU_008G000800g  hypothetical protein [KO:K00162] [EC:1.2.4.1]
PHAVU_006G165600g  hypothetical protein [KO:K00162] [EC:1.2.4.1]
PHAVU_007G026300g  hypothetical protein [KO:K00627] [EC:2.3.1.12]
PHAVU_010G134600g  hypothetical protein [KO:K00627] [EC:2.3.1.12]
PHAVU_007G106200g  hypothetical protein [KO:K00627] [EC:2.3.1.12]
PHAVU_007G090300g  hypothetical protein [KO:K00627] [EC:2.3.1.12]
PHAVU_003G035200g  hypothetical protein [KO:K00627] [EC:2.3.1.12]
PHAVU_007G011400g  hypothetical protein [KO:K00164] [EC:1.2.4.2]
PHAVU_008G014400g  hypothetical protein [KO:K00164] [EC:1.2.4.2]
PHAVU_008G269300g  hypothetical protein [KO:K00658] [EC:2.3.1.61]
PHAVU_009G132900g  hypothetical protein [KO:K00166] [EC:1.2.4.4]
PHAVU_009G156400g  hypothetical protein [KO:K00166] [EC:1.2.4.4]
PHAVU_010G0177000  hypothetical protein [KO:K00167] [EC:1.2.4.4]
PHAVU_003G106700g  hypothetical protein [KO:K09699] [EC:2.3.1.168]
PHAVU_001G035500g  hypothetical protein [KO:K00281] [EC:1.4.4.2]
PHAVU_009G077400g  hypothetical protein [KO:K00281] [EC:1.4.4.2]
PHAVU_003G080400g  hypothetical protein [KO:K00605] [EC:2.1.2.10]
PHAVU_006G148700g  hypothetical protein [KO:K00605] [EC:2.1.2.10]
PHAVU_003G122000g  hypothetical protein [KO:K02437]
PHAVU_002G006000g  hypothetical protein [KO:K02437]
PHAVU_007G233300g  hypothetical protein [KO:K02437]
Compound
C00011  CO2
C00014  Ammonia
C00022  Pyruvate
C00024  Acetyl-CoA
C00026  2-Oxoglutarate
C00037  Glycine
C00068  Thiamin diphosphate
C00091  Succinyl-CoA
C00101  Tetrahydrofolate
C00141  3-Methyl-2-oxobutanoic acid
C00143  5,10-Methylenetetrahydrofolate
C00233  4-Methyl-2-oxopentanoate
C00322  2-Oxoadipate
C00527  Glutaryl-CoA
C00630  2-Methylpropanoyl-CoA
C00671  (S)-3-Methyl-2-oxopentanoic acid
C01242  [Protein]-S8-aminomethyldihydrolipoyllysine
C01944  Octanoyl-CoA
C02051  Lipoylprotein
C02147  Dihydrolipoate
C02939  3-Methylbutanoyl-CoA
C02972  Dihydrolipoylprotein
C05125  2-(alpha-Hydroxyethyl)thiamine diphosphate
C05381  3-Carboxy-1-hydroxypropyl-ThPP
C05752  Octanoyl-[acp]
C06157  [Dihydrolipoyllysine-residue succinyltransferase] S-glutaryldihydrolipoyllysine
C06423  Octanoic acid
C15972  Enzyme N6-(lipoyl)lysine
C15973  Enzyme N6-(dihydrolipoyl)lysine
C15974  3-Methyl-1-hydroxybutyl-ThPP
C15975  [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(3-methylbutanoyl)dihydrolipoyllysine
C15976  2-Methyl-1-hydroxypropyl-ThPP
C15977  [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylpropanoyl)dihydrolipoyllysine
C15978  2-Methyl-1-hydroxybutyl-ThPP
C15979  [Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase] S-(2-methylbutanoyl)dihydrolipoyllysine
C15980  (S)-2-Methylbutanoyl-CoA
C16238  Lipoyl-AMP
C16241  (R)-Lipoate
C16254  [Dihydrolipoyllysine-residue succinyltransferase] S-succinyldihydrolipoyllysine
C16255  [Dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine
C22159  [Glycine cleavage system H]-N6-octanoyl-L-lysine
C22160  [Lipoyl-carrier protein E2]-N6-octanoyl-L-lysine
C22161  Dihydrolipoyl-AMP
C22667  4-Carboxy-1-hydroxybutyryl-ThPP
Reference
  Authors
Gunther S, McMillan PJ, Wallace LJ, Muller S.
  Title
Plasmodium falciparum possesses organelle-specific alpha-keto acid dehydrogenase complexes and lipoylation pathways.
  Journal
Biochem Soc Trans 33:977-80 (2005)
DOI:10.1042/BST20050977
Reference
  Authors
Fujiwara K, Takeuchi S, Okamura-Ikeda K, Motokawa Y.
  Title
Purification, characterization, and cDNA cloning of lipoate-activating enzyme from bovine liver.
  Journal
J Biol Chem 276:28819-23 (2001)
DOI:10.1074/jbc.M101748200
Reference
PMID:9808738
  Authors
Yasuno R, Wada H.
  Title
Biosynthesis of lipoic acid in Arabidopsis: cloning and characterization of the cDNA for lipoic acid synthase.
  Journal
Plant Physiol 118:935-43 (1998)
DOI:10.1104/pp.118.3.935
Reference
  Authors
Gueguen V, Macherel D, Jaquinod M, Douce R, Bourguignon J.
  Title
Fatty acid and lipoic acid biosynthesis in higher plant mitochondria.
  Journal
J Biol Chem 275:5016-25 (2000)
DOI:10.1074/jbc.275.7.5016
Reference
  Authors
Wada M, Yasuno R, Jordan SW, Cronan JE Jr, Wada H.
  Title
Lipoic acid metabolism in Arabidopsis thaliana: cloning and characterization of a cDNA encoding lipoyltransferase.
  Journal
Plant Cell Physiol 42:650-6 (2001)
DOI:10.1093/pcp/pce081
Reference
PMID:8206909
  Authors
Morris TW, Reed KE, Cronan JE Jr.
  Title
Identification of the gene encoding lipoate-protein ligase A of Escherichia coli. Molecular cloning and characterization of the lplA gene and gene product.
  Journal
J Biol Chem 269:16091-100 (1994)
Reference
  Authors
Zhao X, Miller JR, Jiang Y, Marletta MA, Cronan JE.
  Title
Assembly of the covalent linkage between lipoic acid and its cognate enzymes.
  Journal
Chem Biol 10:1293-302 (2003)
DOI:10.1016/j.chembiol.2003.11.016
Reference
  Authors
Nesbitt NM, Baleanu-Gogonea C, Cicchillo RM, Goodson K, Iwig DF, Broadwater JA, Haas JA, Fox BG, Booker SJ.
  Title
Expression, purification, and physical characterization of Escherichia coli lipoyl(octanoyl)transferase.
  Journal
Protein Expr Purif 39:269-82 (2005)
DOI:10.1016/j.pep.2004.10.021
Reference
  Authors
Solmonson A, DeBerardinis RJ
  Title
Lipoic acid metabolism and mitochondrial redox regulation.
  Journal
J Biol Chem 293:7522-7530 (2018)
DOI:10.1074/jbc.TM117.000259
Reference
  Authors
Cronan JE
  Title
Assembly of Lipoic Acid on Its Cognate Enzymes: an Extraordinary and Essential Biosynthetic Pathway.
  Journal
Microbiol Mol Biol Rev 80:429-50 (2016)
DOI:10.1128/MMBR.00073-15
Reference
  Authors
Mayr JA, Feichtinger RG, Tort F, Ribes A, Sperl W
  Title
Lipoic acid biosynthesis defects.
  Journal
J Inherit Metab Dis 37:553-63 (2014)
DOI:10.1007/s10545-014-9705-8
Reference
  Authors
Cao X, Zhu L, Song X, Hu Z, Cronan JE
  Title
Protein moonlighting elucidates the essential human pathway catalyzing lipoic acid assembly on its cognate enzymes.
  Journal
Proc Natl Acad Sci U S A 115:E7063-E7072 (2018)
DOI:10.1073/pnas.1805862115
Reference
  Authors
Soreze Y, Boutron A, Habarou F, Barnerias C, Nonnenmacher L, Delpech H, Mamoune A, Chretien D, Hubert L, Bole-Feysot C, Nitschke P, Correia I, Sardet C, Boddaert N, Hamel Y, Delahodde A, Ottolenghi C, de Lonlay P
  Title
Mutations in human lipoyltransferase gene LIPT1 cause a Leigh disease with secondary deficiency for pyruvate and alpha-ketoglutarate dehydrogenase.
  Journal
Orphanet J Rare Dis 8:192 (2013)
DOI:10.1186/1750-1172-8-192
Reference
  Authors
Habarou F, Hamel Y, Haack TB, Feichtinger RG, Lebigot E, Marquardt I, Busiah K, Laroche C, Madrange M, Grisel C, Pontoizeau C, Eisermann M, Boutron A, Chretien D, Chadefaux-Vekemans B, Barouki R, Bole-Feysot C, Nitschke P, Goudin N, Boddaert N, Nemazanyy I, Delahodde A, Kolker S, Rodenburg RJ, Korenke GC, Meitinger T, Strom TM, Prokisch H, Rotig A, Ottolenghi C, Mayr JA, de Lonlay P
  Title
Biallelic Mutations in LIPT2 Cause a Mitochondrial Lipoylation Defect Associated with Severe Neonatal Encephalopathy.
  Journal
Am J Hum Genet 101:283-290 (2017)
DOI:10.1016/j.ajhg.2017.07.001
Reference
  Authors
Spalding MD, Prigge ST
  Title
Lipoic acid metabolism in microbial pathogens.
  Journal
Microbiol Mol Biol Rev 74:200-28 (2010)
DOI:10.1128/MMBR.00008-10
Reference
  Authors
Guerra AJ, Afanador GA, Prigge ST
  Title
Crystal structure of lipoate-bound lipoate ligase 1, LipL1, from Plasmodium falciparum.
  Journal
Proteins 85:1777-1783 (2017)
DOI:10.1002/prot.25324
Reference
  Authors
Afanador GA, Matthews KA, Bartee D, Gisselberg JE, Walters MS, Freel Meyers CL, Prigge ST
  Title
Redox-dependent lipoylation of mitochondrial proteins in Plasmodium falciparum.
  Journal
Mol Microbiol 94:156-71 (2014)
DOI:10.1111/mmi.12753
Reference
  Authors
Afanador GA, Guerra AJ, Swift RP, Rodriguez RE, Bartee D, Matthews KA, Schon A, Freire E, Freel Meyers CL, Prigge ST
  Title
A novel lipoate attachment enzyme is shared by Plasmodium and Chlamydia species.
  Journal
Mol Microbiol 106:439-451 (2017)
DOI:10.1111/mmi.13776
Reference
  Authors
Storm J, Muller S
  Title
Lipoic acid metabolism of Plasmodium--a suitable drug target.
  Journal
Curr Pharm Des 18:3480-9 (2012)
DOI:10.2174/138161212801327266
Reference
  Authors
Gunther S, Wallace L, Patzewitz EM, McMillan PJ, Storm J, Wrenger C, Bissett R, Smith TK, Muller S
  Title
Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.
  Journal
PLoS Pathog 3:e189 (2007)
DOI:10.1371/journal.ppat.0030189
Reference
  Authors
Wrenger C, Muller S
  Title
The human malaria parasite Plasmodium falciparum has distinct organelle-specific lipoylation pathways.
  Journal
Mol Microbiol 53:103-13 (2004)
DOI:10.1111/j.1365-2958.2004.04112.x
Reference
  Authors
Martin N, Christensen QH, Mansilla MC, Cronan JE, de Mendoza D
  Title
A novel two-gene requirement for the octanoyltransfer reaction of Bacillus subtilis lipoic acid biosynthesis.
  Journal
Mol Microbiol 80:335-49 (2011)
DOI:10.1111/j.1365-2958.2011.07597.x
Reference
  Authors
Christensen QH, Martin N, Mansilla MC, de Mendoza D, Cronan JE
  Title
A novel amidotransferase required for lipoic acid cofactor assembly in Bacillus subtilis.
  Journal
Mol Microbiol 80:350-63 (2011)
DOI:10.1111/j.1365-2958.2011.07598.x
Related
pathway
pvu00020  Citrate cycle (TCA cycle)
pvu00061  Fatty acid biosynthesis
pvu00260  Glycine, serine and threonine metabolism
pvu00280  Valine, leucine and isoleucine degradation
pvu00310  Lysine degradation
pvu00620  Pyruvate metabolism
KO pathway
ko00785   
LinkDB

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