KEGG   PATHWAY: ebw00270Help
Entry
ebw00270                    Pathway                                

Name
Cysteine and methionine metabolism - Escherichia coli BW2952
Description
Cysteine and methionine are sulfur-containing amino acids. Cysteine is synthesized from serine through different pathways in different organism groups. In bacteria and plants, cysteine is converted from serine (via acetylserine) by transfer of hydrogen sulfide [MD:M00021]. In animals, methionine-derived homocysteine is used as sulfur source and its condensation product with serine (cystathionine) is converted to cysteine [MD:M00338]. Cysteine is metabolized to pyruvate in multiple routes. Methionine is an essential amino acid, which animals cannot synthesize. In bacteria and plants, methionine is synthesized from aspartate [MD:M00017]. S-Adenosylmethionine (SAM), synthesized from methionine and ATP, is a methyl group donor in many important transfer reactions including DNA methylation for regulation of gene expression. SAM may also be used to regenerate methionine in the methionine salvage pathway [MD:M00034].
Class
Metabolism; Amino acid metabolism
BRITE hierarchy
Pathway map
ebw00270  Cysteine and methionine metabolism
ebw00270

Ortholog table
Module
ebw_M00017  Methionine biosynthesis, apartate => homoserine => methionine [PATH:ebw00270]
ebw_M00021  Cysteine biosynthesis, serine => cysteine [PATH:ebw00270]
Other DBs
BSID: 104462
GO: 0006534 0006555
Organism
Escherichia coli BW2952 [GN:ebw]
Gene
BWG_3298  cysE; serine acetyltransferase [KO:K00640] [EC:2.3.1.30]
BWG_2176  cysK; cysteine synthase A, O-acetylserine sulfhydrolase A subunit [KO:K01738] [EC:2.5.1.47]
BWG_2183  cysM; cysteine synthase B (O-acetylserine sulfhydrolase B) [KO:K12339] [EC:2.5.1.47]
BWG_2722  metC; cystathionine beta-lyase, PLP-dependent [KO:K01760] [EC:4.4.1.8]
BWG_1436  malY; bifunctional beta-cystathionase, PLP-dependent/regulator of maltose regulon [KO:K14155] [EC:4.4.1.8]
BWG_3675  metH; homocysteine-N5-methyltetrahydrofolate transmethylase, B12-dependent [KO:K00548] [EC:2.1.1.13]
BWG_3507  metE; 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase [KO:K00549] [EC:2.1.1.14]
BWG_2664  metK; methionine adenosyltransferase 1 [KO:K00789] [EC:2.5.1.6]
BWG_0113  speD; S-adenosylmethionine decarboxylase [KO:K01611] [EC:4.1.1.50]
BWG_0114  speE; spermidine synthase (putrescine aminopropyltransferase) [KO:K00797] [EC:2.5.1.16]
BWG_0152  mtn; 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase [KO:K01243] [EC:3.2.2.9]
BWG_3767  tyrB; tyrosine aminotransferase, tyrosine-repressible, PLP-dependent [KO:K00832] [EC:2.6.1.57]
BWG_1765  dcm; DNA cytosine methylase [KO:K00558] [EC:2.1.1.37]
BWG_2428  luxS; S-ribosylhomocysteinase [KO:K07173] [EC:4.4.1.21]
BWG_3680  lysC; aspartokinase III [KO:K00928] [EC:2.7.2.4]
BWG_0002  thrA; fused aspartokinase I and homoserine dehydrogenase I [KO:K12524] [EC:1.1.1.3 2.7.2.4]
BWG_3609  metL; fused aspartokinase II/homoserine dehydrogenase II [KO:K12525] [EC:1.1.1.3 2.7.2.4]
BWG_3125  asd; aspartate-semialdehyde dehydrogenase, NAD(P)-binding [KO:K00133] [EC:1.2.1.11]
BWG_3669  metA; homoserine O-transsuccinylase [KO:K00651] [EC:2.3.1.31 2.3.1.46]
BWG_3608  metB; cystathionine gamma-synthase, PLP-dependent [KO:K01739] [EC:2.5.1.48]
BWG_3455  ilvE; branched-chain amino-acid aminotransferase [KO:K00826] [EC:2.6.1.42]
BWG_2429  gshA; gamma-glutamate-cysteine ligase [KO:K01919] [EC:6.3.2.2]
BWG_2669  gshB; glutathione synthetase [KO:K01920] [EC:6.3.2.3]
BWG_0780  aspC; aspartate aminotransferase, PLP-dependent [KO:K00813] [EC:2.6.1.1]
BWG_2285  sseA; 3-mercaptopyruvate sulfurtransferase [KO:K01011] [EC:2.8.1.2 2.8.1.1]
BWG_1728  dcyD; D-cysteine desulfhydrase, PLP-dependent [KO:K05396] [EC:4.4.1.15]
BWG_2937  mdh; malate dehydrogenase, NAD(P)-binding [KO:K00024] [EC:1.1.1.37]
BWG_2535  sdaB; L-serine deaminase II [KO:K01752] [EC:4.3.1.17]
BWG_2820  tdcG; L-serine dehydratase 3 [KO:K01752] [EC:4.3.1.17]
BWG_1627  sdaA; L-serine deaminase I [KO:K01752] [EC:4.3.1.17]
BWG_1646  yebR; free methionine-(R)-sulfoxide reductase [KO:K08968] [EC:1.8.4.14]
Compound
C00019  S-Adenosyl-L-methionine
C00021  S-Adenosyl-L-homocysteine
C00022  Pyruvate
C00041  L-Alanine
C00049  L-Aspartate
C00051  Glutathione
C00059  Sulfate
C00065  L-Serine
C00073  L-Methionine
C00094  Sulfite
C00097  L-Cysteine
C00109  2-Oxobutanoate
C00155  L-Homocysteine
C00170  5'-Methylthioadenosine
C00263  L-Homoserine
C00283  Hydrogen sulfide
C00409  Methanethiol
C00441  L-Aspartate 4-semialdehyde
C00491  L-Cystine
C00506  L-Cysteate
C00606  3-Sulfino-L-alanine
C00793  D-Cysteine
C00957  Mercaptopyruvate
C00979  O-Acetyl-L-serine
C01005  O-Phospho-L-serine
C01077  O-Acetyl-L-homoserine
C01118  O-Succinyl-L-homoserine
C01137  S-Adenosylmethioninamine
C01180  4-Methylthio-2-oxobutanoic acid
C01234  1-Aminocyclopropane-1-carboxylate
C01817  L-Homocystine
C01962  Thiocysteine
C02218  Dehydroalanine
C02291  L-Cystathionine
C02356  (S)-2-Aminobutanoate
C02989  L-Methionine S-oxide
C03082  4-Phospho-L-aspartate
C03089  5-Methylthio-D-ribose
C03145  N-Formylmethionine
C03539  S-Ribosyl-L-homocysteine
C04188  S-Methyl-5-thio-D-ribose 1-phosphate
C04582  S-Methyl-5-thio-D-ribulose 1-phosphate
C05524  Aminoacyl-L-methionine
C05526  S-Glutathionyl-L-cysteine
C05527  3-Sulfinylpyruvate
C05528  3-Sulfopyruvate
C05823  3-Mercaptolactate
C05824  S-Sulfo-L-cysteine
C06547  Ethylene
C08276  3-(Methylthio)propanoate
C09306  Sulfur dioxide
C11481  HSO3-
C11499  (S)-3-Sulfolactate
C11537  (2R)-3-Sulfolactate
C15606  1,2-Dihydroxy-5-(methylthio)pent-1-en-3-one
C15650  2,3-Diketo-5-methylthiopentyl-1-phosphate
C15651  2-Hydroxy-3-keto-5-methylthiopentenyl-1-phosphate
C18049  N-Acyl-L-homoserine lactone
C19787  5'-S-Methyl-5'-thioinosine
C21015  gamma-L-Glutamyl-L-2-aminobutyrate
C21016  Ophthalmate
Reference
  Authors
Sekowska A, Denervaud V, Ashida H, Michoud K, Haas D, Yokota A, Danchin A
  Title
Bacterial variations on the methionine salvage pathway.
  Journal
BMC Microbiol 4:9 (2004)
DOI:10.1186/1471-2180-4-9
Reference
  Authors
Ashida H, Saito Y, Kojima C, Kobayashi K, Ogasawara N, Yokota A.
  Title
A functional link between RuBisCO-like protein of Bacillus and photosynthetic RuBisCO.
  Journal
Science 302:286-90 (2003)
DOI:10.1126/science.1086997
Reference
  Authors
Sekowska A, Danchin A.
  Title
The methionine salvage pathway in Bacillus subtilis.
  Journal
BMC Microbiol 2:8 (2002)
DOI:10.1186/1471-2180-2-8
Reference
  Authors
Berger BJ, English S, Chan G, Knodel MH.
  Title
Methionine regeneration and aminotransferases in Bacillus subtilis, Bacillus cereus, and Bacillus anthracis.
  Journal
J Bacteriol 185:2418-31 (2003)
DOI:10.1128/JB.185.8.2418-2431.2003
Reference
  Authors
Goyer A, Collakova E, Shachar-Hill Y, Hanson AD
  Title
Functional characterization of a methionine gamma-lyase in Arabidopsis and its implication in an alternative to the reverse trans-sulfuration pathway.
  Journal
Plant Cell Physiol 48:232-42 (2007)
DOI:10.1093/pcp/pcl055
Reference
  Authors
Rebeille F, Jabrin S, Bligny R, Loizeau K, Gambonnet B, Van Wilder V, Douce R, Ravanel S
  Title
Methionine catabolism in Arabidopsis cells is initiated by a gamma-cleavage process and leads to S-methylcysteine and isoleucine syntheses.
  Journal
Proc Natl Acad Sci U S A 103:15687-92 (2006)
DOI:10.1073/pnas.0606195103
Reference
  Authors
Pirkov I, Norbeck J, Gustafsson L, Albers E
  Title
A complete inventory of all enzymes in the eukaryotic methionine salvage pathway.
  Journal
FEBS J 275:4111-20 (2008)
DOI:10.1111/j.1742-4658.2008.06552.x
Reference
  Authors
Ashida H, Saito Y, Kojima C, Yokota A
  Title
Enzymatic characterization of 5-methylthioribulose-1-phosphate dehydratase of the methionine salvage pathway in Bacillus subtilis.
  Journal
Biosci Biotechnol Biochem 72:959-67 (2008)
DOI:10.1271/bbb.70651
Reference
  Authors
Kitabatake M, So MW, Tumbula DL, Soll D
  Title
Cysteine biosynthesis pathway in the archaeon Methanosarcina barkeri encoded by acquired bacterial genes?
  Journal
J Bacteriol 182:143-5 (2000)
DOI:10.1128/JB.182.1.143-145.2000
Reference
  Authors
Mino K, Ishikawa K
  Title
Characterization of a novel thermostable O-acetylserine sulfhydrylase from Aeropyrum pernix K1.
  Journal
J Bacteriol 185:2277-84 (2003)
DOI:10.1128/JB.185.7.2277-2284.2003
Reference
  Authors
Tanabe S
  Title
Development of assay methods for endogenous inorganic sulfur compounds and sulfurtransferases and evaluation of the physiological functions of bound sulfur.
  Journal
Yakugaku Zasshi 128:881-900 (2008)
DOI:10.1248/yakushi.128.881
Reference
  Authors
Nishizuka Y, Seyama Y, Ikai A, Ishimura Y, Kawaguchi A (eds).
  Title
[Cellular Functions and Metabolic Maps] (In Japanese)
  Journal
Tokyo Kagaku Dojin (1997)
Reference
  Authors
Gutierrez JA, Crowder T, Rinaldo-Matthis A, Ho MC, Almo SC, Schramm VL
  Title
Transition state analogs of 5'-methylthioadenosine nucleosidase disrupt quorum sensing.
  Journal
Nat Chem Biol 5:251-7 (2009)
DOI:10.1038/nchembio.153
KO pathway
ko00270   

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