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MetaCyc Pathway: alanine degradation II (to D-lactate)

This view shows enzymes only for those organisms listed below, in the list of taxa known to possess the pathway. If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.

Superclasses: Degradation/Utilization/Assimilation Amino Acids Degradation Alanine Degradation

Some taxa known to possess this pathway include ? : [Clostridium] propionicum

Expected Taxonomic Range: Firmicutes , Viridiplantae

Summary:
Some anaerobic bacteria can ferment amino acids. [Clostridium] propionicum can ferment L-alanine as shown in this pathway and the associated pathway link. The amino group of L-alanine is transferred to 2-oxoglutarate, resulting in the formation of pyruvate and L-glutamate. 2-oxoglutarate is regenerated by NAD-dependent glutamate dehydrogenase, producing ammonia.

pyruvate is reduced to (R)-lactate ((R)-lactate), which is subsequently reduced to propanoate. Pyruvate can also be oxidized to acetate and CO2 [Schweiger84, Hetzel03, Selmer02].

For information about the full pathway, see L-alanine fermentation to propionate and acetate.

Superpathways: L-alanine fermentation to propionate and acetate

Variants: alanine degradation I , alanine degradation III , alanine degradation IV

Unification Links: KEGG:MAP00640

Credits:
Created 28-Dec-1998 by Iourovitski I , SRI International
Revised 11-Dec-2006 by Fulcher CA , SRI International


References

Hetzel03: Hetzel M, Brock M, Selmer T, Pierik AJ, Golding BT, Buckel W (2003). "Acryloyl-CoA reductase from Clostridium propionicum. An enzyme complex of propionyl-CoA dehydrogenase and electron-transferring flavoprotein." Eur J Biochem 270(5);902-10. PMID: 12603323

Schweiger84: Schweiger G, Buckel W (1984). "On the dehydration of (R)-lactate in the fermentation of alanine to propionate by Clostridium propionicum." FEBS Lett 1984;171(1);79-84. PMID: 6586495

Selmer02: Selmer T, Willanzheimer A, Hetzel M (2002). "Propionate CoA-transferase from Clostridium propionicum. Cloning of gene and identification of glutamate 324 at the active site." Eur J Biochem 269(1);372-80. PMID: 11784332

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

Bonete89: Bonete MJ, Camacho ML, Cadenas E (1989). "Kinetic mechanism of Halobacterium halobium NAD+-glutamate dehydrogenase." Biochim Biophys Acta 1989;990(2);150-5. PMID: 2917175

Bonete96a: Bonete MJ, Perez-Pomares F, Ferrer J, Camacho ML (1996). "NAD-glutamate dehydrogenase from Halobacterium halobium: inhibition and activation by TCA intermediates and amino acids." Biochim Biophys Acta 1996;1289(1);14-24. PMID: 8605224

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

Bugg91: Bugg TD, Wright GD, Dutka-Malen S, Arthur M, Courvalin P, Walsh CT (1991). "Molecular basis for vancomycin resistance in Enterococcus faecium BM4147: biosynthesis of a depsipeptide peptidoglycan precursor by vancomycin resistance proteins VanH and VanA." Biochemistry 30(43);10408-15. PMID: 1931965

Chae11: Chae, Lee (2011). "The functional annotation of protein sequences was performed by the in-house Ensemble Enzyme Prediction Pipeline (E2P2, version 1.0). E2P2 systematically integrates results from three molecular function annotation algorithms using an ensemble classification scheme. For a given genome, all protein sequences are submitted as individual queries against the base-level annotation methods. The individual methods rely on homology transfer to annotate protein sequences, using single sequence (BLAST, E-value cutoff <= 1e-30, subset of SwissProt 15.3) and multiple sequence (Priam, November 2010; CatFam, version 2.0, 1% FDR profile library) models of enzymatic functions. The base-level predictions are then integrated into a final set of annotations using an average weighted integration algorithm, where the weight of each prediction from each individual method was determined via a 0.632 bootstrap process over 1000 rounds of testing. The training and testing data for E2P2 and the BLAST reference database were drawn from protein sequences with experimental support of existence, compiled from SwissProt release 15.3."

Dartois95: Dartois V, Phalip V, Schmitt P, Divies C (1995). "Purification, properties and DNA sequence of the D-lactate dehydrogenase from Leuconostoc mesenteroides subsp. cremoris." Res Microbiol 146(4);291-302. PMID: 7569323

Ewaschuk05: Ewaschuk JB, Naylor JM, Zello GA (2005). "D-lactate in human and ruminant metabolism." J Nutr 135(7);1619-25. PMID: 15987839

Felbeck80: Felbeck H, Grieshaber MK (1980). "Investigations on some enzymes involved in the anaerobic metabolism of amino acids of Arenicola marina L." Comparative Biochemistry and Physiology Part B: Comparative Biochemistry 66(2);205-213.

Garvie80: Garvie EI (1980). "Bacterial lactate dehydrogenases." Microbiol Rev 44(1);106-39. PMID: 6997721

Gottschalk86: Gottschalk, G "Bacterial Metabolism, Second Edition." Springer-Verlag, New York. 1986.

Ishiguro91: Ishiguro M, Takio K, Suzuki M, Oyama R, Matsuzawa T, Titani K (1991). "Complete amino acid sequence of human liver cytosolic alanine aminotransferase (GPT) determined by a combination of conventional and mass spectral methods." Biochemistry 30(43);10451-7. PMID: 1931970

Janssen91: Janssen PH (1991). "Isolation of Clostridium propionicum strain 19acry3 and further characteristics of the species." Arch Microbiol 1991;155(6);566-71. PMID: 1953298

Kim10: Kim SH, Schneider BL, Reitzer L (2010). "Genetics and regulation of the major enzymes of alanine synthesis in Escherichia coli." J Bacteriol 192(20);5304-11. PMID: 20729367

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

Lerud71: Lerud RF, Whiteley HR (1971). "Purification and properties of alpha-ketoglutarate reductase from Micrococcus aerogenes." J Bacteriol 1971;106(2);571-7. PMID: 4396793

Liepman03: Liepman AH, Olsen LJ (2003). "Alanine aminotransferase homologs catalyze the glutamate:glyoxylate aminotransferase reaction in peroxisomes of Arabidopsis." Plant Physiol 131(1);215-27. PMID: 12529529

MatJan89: Mat-Jan F, Alam KY, Clark DP (1989). "Mutants of Escherichia coli deficient in the fermentative lactate dehydrogenase." J Bacteriol 1989;171(1);342-8. PMID: 2644194

MeloOliveira96: Melo-Oliveira R, Oliveira IC, Coruzzi GM (1996). "Arabidopsis mutant analysis and gene regulation define a nonredundant role for glutamate dehydrogenase in nitrogen assimilation." Proc Natl Acad Sci U S A 93(10);4718-23. PMID: 8643469

Miller91: Miller SM, Magasanik B (1991). "Role of the complex upstream region of the GDH2 gene in nitrogen regulation of the NAD-linked glutamate dehydrogenase in Saccharomyces cerevisiae." Mol Cell Biol 11(12);6229-47. PMID: 1682801

Moat95: Moat, AG, Foster, JW "Microbial Physiology, Third Edition." Wiley-Liss, New York. 1995.

Showing only 20 references. To show more, press the button "Show all references".


Report Errors or Provide Feedback
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 Fri Nov 28, 2014, BIOCYC13B.