If an enzyme name is shown in bold, there is experimental evidence for this enzymatic activity.
Locations of Mapped Genes:
|Superclasses:||Biosynthesis → Amino Acids Biosynthesis → Proteinogenic Amino Acids Biosynthesis → L-alanine Biosynthesis|
Alanine is an essential component of protein (as L-alanine) and peptidoglycan (as a roughly 3:1 mix of D- and L-alanine). Only about a tenth of total alanine synthesized is incorporated into peptidoglycan.
At least three pathways ( L-alanine biosynthesis I, L-alanine biosynthesis II, and L-alanine biosynthesis III) contribute to the synthesis of alanine. The specific contribution of alanine biosynthesis I to overall alanine production in the cell remains unclear, given that it consists of a series of reversible reactions involved in other physiological processes, and alanine auxotrophs based on this pathway have not been generated.
Superpathways: superpathway of L-alanine biosynthesis
LeePeng79: Lee-Peng FC, Hermodson MA, Kohlhaw GB (1979). "Transaminase B from Escherichia coli: quaternary structure, amino-terminal sequence, substrate specificity, and absence of a separate valine-alpha-ketoglutarate activity." J Bacteriol 1979;139(2);339-45. PMID: 378964
Berg88: Berg CM, Wang MD, Vartak NB, Liu L (1988). "Acquisition of new metabolic capabilities: multicopy suppression by cloned transaminase genes in Escherichia coli K-12." Gene 65(2);195-202. PMID: 3044925
Cho03: Cho BK, Cho HJ, Park SH, Yun H, Kim BG (2003). "Simultaneous synthesis of enantiomerically pure (S)-amino acids and (R)-amines using coupled transaminase reactions." Biotechnol Bioeng 81(7);783-9. PMID: 12557311
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
Falkinham77: Falkinham JO (1977). "Escherichia coli K-12 mutant with alternate requirements for vitamin B6 or branched-chain amino acids and lacking transaminase C activity." J Bacteriol 130(1);566-8. PMID: 323243
Goto03: Goto M, Miyahara I, Hayashi H, Kagamiyama H, Hirotsu K (2003). "Crystal structures of branched-chain amino acid aminotransferase complexed with glutamate and glutarate: true reaction intermediate and double substrate recognition of the enzyme." Biochemistry 42(13);3725-33. PMID: 12667063
Inoue88a: Inoue K, Kuramitsu S, Aki K, Watanabe Y, Takagi T, Nishigai M, Ikai A, Kagamiyama H (1988). "Branched-chain amino acid aminotransferase of Escherichia coli: overproduction and properties." J Biochem (Tokyo) 1988;104(5);777-84. PMID: 3069843
Jamindar10: Jamindar D, Gutheil WG (2010). "A liquid chromatography-tandem mass spectrometry assay for Marfey's derivatives of L-Ala, D-Ala, and D-Ala-D-Ala: application to the in vivo confirmation of alanine racemase as the target of cycloserine in Escherichia coli." Anal Biochem 396(1);1-7. PMID: 19748470
Ju11: Ju J, Xu S, Furukawa Y, Zhang Y, Misono H, Minamino T, Namba K, Zhao B, Ohnishi K (2011). "Correlation between catalytic activity and monomer-dimer equilibrium of bacterial alanine racemases." J Biochem 149(1);83-9. PMID: 20971724
Kim03: Kim MG, Strych U, Krause K, Benedik M, Kohn H (2003). "N(2)-substituted D,L-cycloserine derivatives: synthesis and evaluation as alanine racemase inhibitors." J Antibiot (Tokyo) 56(2);160-8. PMID: 12715876
Showing only 20 references. To show more, press the button "Show all references".
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493