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MetaCyc Enzyme: sarcosine oxidase

Gene: soxA Accession Number: G-8522 (MetaCyc)

Species: Arthrobacter sp. TE1826

Summary:
The sarcosine oxidase from Arthrobacter sp. TE1826 is encoded by the soxA gene, a part of a creatinine degradation operon, which also contains the genes for creatininase (crnA) and creatinase (creA), a regulator (soxR) and two putative transporters [Nishiya98].

The protein was purified from its native host, and the gene encoding it was cloned and expressed in Escherichia coli and Bacillus subtilis. While the protein is produced in its native host only in the presence of sarcosine, the heterologous hosts produce it constitutively, indicating that a regulatory region that is recognized by Arthrobacter is not recognized in the otehr organisms [Nishiya93].

The enzyme was later subjected to site-directed mutagenesis in an attempt to alter its substrate specificity and optimum pH [Nishiya94]. Five different mutants in position 103 (originally phenylalanine) were generated, with striking differences in substrate specificity [Nishiya94].

Locations: cytosol

Molecular Weight of Polypeptide: 43.249 kD (from nucleotide sequence), 43 kD (experimental) [Nishiya93 ]

Unification Links: ModBase:P40873 , Protein Model Portal:P40873 , SMR:P40873 , Swiss-Model:P40873 , UniProt:P40873

Relationship Links: Entrez-Nucleotide:RELATED-TO:AB007122 , InterPro:IN-FAMILY:IPR006076 , InterPro:IN-FAMILY:IPR006281 , Pfam:IN-FAMILY:PF01266

Gene-Reaction Schematic: ?

Escherichia coli K-12 substr. MG1655 Pathway: Cellular Component:superpathway of serine and glycine biosynthesis I
GO:0005829 - cytosol [ onMouseOver="return overlib(' Nishiya, Y., Imanaka, T. (1993). "Cloning and sequencing of the sarcosine oxidase gene from Arthrobacter sp. TE1826." J. Ferment. bioeng. 75 (4):239-244.', WIDTH, 500);" onmouseout="return nd();">
Nishiya93]If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.?
MultiFun Terms: metabolism degradation of macromolecules degradation of macromolecules

Genetic Regulation Schematic:
Locations of Mapped Genes:proteins/peptides/glycopeptides

EC Number: 1.5.3.1EC Number: 1.5.3.1
Superclasses:
Biosynthesis
Amino Acids Biosynthesis
Superpathways

Enzymatic reaction of: sarcosine oxidase

Subpathways: serine biosynthesis , glycine biosynthesis I sarcosine + oxygen + H2O <=> glycine + formaldehyde + hydrogen peroxide The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system. The reaction is physiologically favored in the direction shown. In Pathways: creatinine degradation I Cofactors or Prosthetic Groups: FAD [Nishiya93] Inhibitors (Unknown Mechanism): Ag+ [Nishiya93], Hg2+ [Nishiya93], p-chloromercuribenzoate [Nishiya93]Kinetic Parameters:
onClick="location.href='/ECOLI/NEW-IMAGE?type=PATHWAY&object=SER-GLYSYN-PWY&show-citations=NIL'" >: onMouseOver="return overlib('24516157', WIDTH, 68);" onmouseout="return nd();">Blank14: : : 7.5 Burton08: [ Burton RL, Hanes JW, Grant GA (2008). "A stopped flow transient kinetic analysis of substrate binding and catalysis in Escherichia coli D-3-phosphoglycerate dehydrogenase." J Biol Chem 283(44);29706-14. PMID: 18776184 onMouseOver="return overlib('7642604', WIDTH, 62);" onmouseout="return nd();"> Nishiya93: onMouseOver="return overlib('10858298', WIDTH, 68);" onmouseout="return nd();"> Contestabile00 Nishiya, Y., Imanaka, T. (1993). "Cloning and sequencing of the sarcosine oxidase gene from : Arthrobacter sp. TE1826." J. Ferment. bioeng. 75 (4):239-244. Nishiya94: Nishiya Y, Toda A, Imanaka T (1998). "Gene cluster for creatinine degradation in Arthrobacter sp. TE1826." Mol Gen Genet 257(5);581-6. PMID: 9563845 Dubrow77: Dubrow R, Pizer LI (1977). "Transient kinetic studies on the allosteric transition of phosphoglycerate dehydrogenase." J Biol Chem 1977;252(5);1527-38. PMID: 320209 Duncan86: Duncan K, Coggins JR (1986). "The serC-aro A operon of Escherichia coli. A mixed function operon encoding enzymes from two different amino acid biosynthetic pathways." Biochem J 1986;234(1);49-57. PMID: 3518706 ECOSAL: "Escherichia coli and Salmonella: Cellular and Molecular Biology." Online edition. Florio09: Florio R, Chiaraluce R, Consalvi V, Paiardini A, Catacchio B, Bossa F, Contestabile R (2009). "The role of evolutionarily conserved hydrophobic contacts in the quaternary structure stability of Escherichia coli serine hydroxymethyltransferase." FEBS J 276(1);132-43. PMID: 19019081 Florio09a: Florio R, Chiaraluce R, Consalvi V, Paiardini A, Catacchio B, Bossa F, Contestabile R (2009). "Structural stability of the cofactor binding site in Escherichia coli serine hydroxymethyltransferase--the role of evolutionarily conserved hydrophobic contacts." FEBS J 276(24);7319-28. PMID: 19909338 Herrington13: Herrington MB, Sitaras C (2013). "The influence of CsgD on the expression of genes of folate metabolism and hmp in Escherichia coli K-12." Arch Microbiol 195(8);559-69. PMID: 23824318 Hopkins86: Hopkins S, Schirch V (1986). "Properties of a serine hydroxymethyltransferase in which an active site histidine has been changed to an asparagine by site-directed mutagenesis." J Biol Chem 1986;261(7);3363-9. PMID: 3512553 JoshiTope90: Joshi-Tope G, Schirch V (1990). "The role of a critical sulfhydryl group in the mechanism of serine hydroxymethyltransferase." Ann N Y Acad Sci 585;339-45. PMID: 2113366 Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394 Kuznetsova06: Kuznetsova E, Proudfoot M, Gonzalez CF, Brown G, Omelchenko MV, Borozan I, Carmel L, Wolf YI, Mori H, Savchenko AV, Arrowsmith CH, Koonin EV, Edwards AM, Yakunin AF (2006). "Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family." J Biol Chem 281(47):36149-61. PMID: 16990279 [Bairoch93: Bairoch A, Boeckmann B (1993). "The SWISS-PROT protein sequence data bank, recent developments." Nucleic Acids Res. 21:3093-3096. PMID: 8332529 pH(opt) Blank D, Wolf L, Ackermann M, Silander OK (2014). "The predictability of molecular evolution during functional innovation." Proc Natl Acad Sci U S A 111(8);3044-9. PMID: 24516157Cai95: References Cai K, Schirch D, Schirch V (1995). "The affinity of pyridoxal 5'-phosphate for folding intermediates of Escherichia coli serine hydroxymethyltransferase." J Biol Chem 270(33);19294-9. PMID: 7642604 Cai K, Schirch D, Schirch V (1995). "The affinity of pyridoxal 5'-phosphate for folding intermediates of Escherichia coli serine hydroxymethyltransferase." J Biol Chem 270(33);19294-9. PMID: 7642604 Contestabile R, Angelaccio S, Bossa F, Wright HT, Scarsdale N, Kazanina G, Schirch V (2000). "Role of tyrosine 65 in the mechanism of serine hydroxymethyltransferase." Biochemistry 39(25);7492-500. PMID: 10858298Delle94: Nishiya98 Delle Fratte S, Iurescia S, Angelaccio S, Bossa F, Schirch V (1994). "The function of arginine 363 as the substrate carboxyl-binding site in Escherichia coli serine hydroxymethyltransferase." Eur J Biochem 225(1);395-401. PMID: 7925461
Substrate
Km (μM)
References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway
Citations
>
sarcosine
Angelaccio92
3600.0
onMouseOver="return overlib(' Nishiya, Y., Imanaka, T. (1994). "Alteration of substrate specificity and optimum pH of sarcosine oxidase by random and site-directed mutagenesis." Appl. and Environ. Mocrobiol. 60 (11):4213-4215.', WIDTH, 500);" onmouseout="return nd();">Nishiya94
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Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Jan 31, 2015, biocyc14.