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Escherichia coli K-12 substr. MG1655 Pathway: ethanolamine utilization

If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Locations of Mapped Genes:

Superclasses: Degradation/Utilization/Assimilation Amines and Polyamines Degradation

Summary:
E. coli can utilize ethanolamine as the sole source of nitrogen and carbon in the presence of external vitamin B12 [Chang75a, Scarlett76, Jones84] . The requirement for a carboxysome-like structure to contain the metabolic enzymes and volatile reaction products has been studied in Salmonella enterica [Penrod06].

Further catabolism of acetaldehyde may be accomplished by a CoA-dependent aldehyde dehydrogenase via acetyl-CoA [Jones84, Jones84a].

Credits:
Created 09-Jun-2010 by Keseler I , SRI International


References

Chang75a: Chang GW, Chang JT (1975). "Evidence for the B12-dependent enzyme ethanolamine deaminase in Salmonella." Nature 254(5496);150-1. PMID: 1090845

Jones84: Jones PW, Turner JM (1984). "Interrelationships between the enzymes of ethanolamine metabolism in Escherichia coli." J Gen Microbiol 1984;130 ( Pt 2);299-308. PMID: 6374020

Jones84a: Jones PW, Turner JM (1984). "A model for the common control of enzymes of ethanolamine catabolism in Escherichia coli." J Gen Microbiol 1984;130 ( Pt 4);849-60. PMID: 6376700

Penrod06: Penrod JT, Roth JR (2006). "Conserving a volatile metabolite: a role for carboxysome-like organelles in Salmonella enterica." J Bacteriol 188(8);2865-74. PMID: 16585748

Scarlett76: Scarlett FA, Turner JM (1976). "Microbial metabolism of amino alcohols. Ethanolamine catabolism mediated by coenzyme B12-dependent ethanolamine ammonia-lyase in Escherichia coli and Klebsiella aerogenes." J Gen Microbiol 95(1);173-6. PMID: 784902

Other References Related to Enzymes, Genes, Subpathways, and Substrates of this Pathway

Akita10: Akita K, Hieda N, Baba N, Kawaguchi S, Sakamoto H, Nakanishi Y, Yamanishi M, Mori K, Toraya T (2010). "Purification and some properties of wild-type and N-terminal-truncated ethanolamine ammonia-lyase of Escherichia coli." J Biochem 147(1);83-93. PMID: 19762342

Babior88: Babior BM (1988). "The mechanism of adenosylcobalamin-dependent rearrangements." Biofactors 1(1);21-6. PMID: 3076429

Blackwell77: Blackwell CM, Scarlett FA, Turner JM (1977). "Microbial metabolism of amino alcohols. Control of formation and stability of partially purified ethanolamine ammonia-lyase in Escherichia coli." J Gen Microbiol 1977;98(1);133-9. PMID: 319195

Blackwell78: Blackwell CM, Turner JM (1978). "Microbial metabolism of amino alcohols. Purification and properties of coenzyme B12-dependent ethanolamine ammonia-lyase of Escherichia coli." Biochem J 1978;175(2);555-63. PMID: 33657

Blackwell78a: Blackwell CM, Turner JM (1978). "Microbial metabolism of amino alcohols. Formation of coenzyme B12-dependent ethanolamine ammonia-lyase and its concerted induction in Escherichia coli." Biochem J 176(3);751-7. PMID: 371614

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

GOA01: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA01a: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

Mori04: Mori K, Bando R, Hieda N, Toraya T (2004). "Identification of a reactivating factor for adenosylcobalamin-dependent ethanolamine ammonia lyase." J Bacteriol 186(20);6845-54. PMID: 15466038

Pennington81: Pennington SJ, Jones PW, Turner JM (1981). "The adenosylcobalamin-dependent ethanolamine ammonia-lyase of Escherichia coli." Biochemical Society Transactions 9:447.

Shibata10: Shibata N, Tamagaki H, Ohtsuki S, Hieda N, Akita K, Komori H, Shomura Y, Terawaki S, Toraya T, Yasuoka N, Higuchi Y (2010). "Expression, crystallization and preliminary X-ray crystallographic study of ethanolamine ammonia-lyase from Escherichia coli." Acta Crystallogr Sect F Struct Biol Cryst Commun 66(Pt 6);709-11. PMID: 20516606

Shibata10a: Shibata N, Tamagaki H, Hieda N, Akita K, Komori H, Shomura Y, Terawaki S, Mori K, Yasuoka N, Higuchi Y, Toraya T (2010). "Crystal structures of ethanolamine ammonia-lyase complexed with coenzyme B12 analogs and substrates." J Biol Chem 285(34);26484-93. PMID: 20519496

Shibata11: Shibata N, Higuchi Y, Toraya T (2011). "How coenzyme B12-dependent ethanolamine ammonia-lyase deals with both enantiomers of 2-amino-1-propanol as substrates: structure-based rationalization." Biochemistry 50(4);591-8. PMID: 21142024

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Wed Nov 26, 2014, biocyc13.