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.
Synonyms: sym-norspermidine biosynthesis
|Superclasses:||Biosynthesis → Amines and Polyamines Biosynthesis|
Some taxa known to possess this pathway include : Vibrio alginolyticus , Vibrio alginolyticus NBRC 15630 = ATCC 17749 , Vibrio cholerae , Vibrio parahaemolyticus , Vibrio vulnificus , Vibrio vulnificus CMCP6
Expected Taxonomic Range: Vibrionaceae
Polyamines are found in bacteria, archaea and eukaryotes and are necessary for normal cellular physiology. They include the diamine putrescine, the triamines spermidine, norspermidine (sym-norspermidine) and sym-homospermidine (homospermidine) and the tetraamine spermine (in [Shaw10] and in [Lee09]). Links to their biosynthetic pathways can be found by clicking on these compounds links. See also superpathway of polyamine biosynthesis I, superpathway of polyamine biosynthesis II and superpathway of polyamine biosynthesis III. In members of the genus Vibrio, norspermidine is a major polyamine (in [Lee09].
About This Pathway
In this pathway L-aspartate-semialdehyde donates a carboxyaminopropyl group to propane-1,3-diamine to form carboxynorspermidine in a reaction catalyzed by carboxynorspermidine/carboxyspermidine dehydrogenase (CANSDH). Decarboxylation of carboxynorspermidine catalyzed by carboxynorspermidine/carboxyspermidine decarboxylase (CANSDC) produces norspermidine. L-aspartate-semialdehyde is also a precursor for propane-1,3-diamine biosynthesis from L-2,4-diaminobutanoate which is catalyzed by a bifunctional fusion protein L-2,4-diaminobutyrate aminotransferase/decarboxylase (DABA AT/DC) ([Yamamoto86, Lee09] and in [Shaw10]).
This L-aspartate-semialdehyde based pathway has been experimentally demonstrated in vivo in Vibrio cholerae including a branch of this pathway that leads to the biosynthesis of spermidine as shown in the pathway link. Both pathways are shown together in superpathway of polyamine biosynthesis III.
Heterologous expression in Escherichia coli of the genes encoding the enzymes in this pathway resulted in accumulation of propane-1,3-diamine and norspermidine (which are inactive polyamines in Escherichia coli). Deletion of the gene encoding CANSDC in Vibrio cholerae resulted in accumulation of carboxynorspermidine. Deletion of the genes encoding either CANSDC or CANSDH led to loss of norspermidine and spermidine, thus identifying the gene encoding CANSDH. Interestingly, deletion of the Vibrio cholerae genes encoding either CANSDH or CANSDC reduced the growth rate of planktonic cells by approximately 50% and severely reduced biofilm formation. Biofilm formation could be rescued by adding exogenous norspermidine, but not spermidine . The pathway did not appear to be related to the infectivity of Vibrio cholerae, using a mouse model [Lee09]. Earlier work also suggested a role for norspermidine in biofilm formation in Vibrio cholerae [Karatan05].
Bioinformatic analysis suggested that DABA AT/DC fusion proteins and their clustering with CANSDH and CANSDC were found only in the family Vibrionaceae, giving support to their role in both spermidine and norspermidine biosynthesis in these organisms. However, a clustered pair of CANSDH and CANSDC genes was widespread in the α-, β-, γ-, δ- and ε-proteobacteria, firmicutes and a candidate division TG-1, suggesting that the pathway for spermidine biosynthesis may be more widely used. However, this conclusion could not be extended to norspermidine biosynthesis without experimental support due to the use of L-2,4-diaminobutanoate in other pathways (see ectoine biosynthesis, pyoverdine I biosynthesis and rhizobactin 1021 biosynthesis) [Lee09].
Superpathways: superpathway of polyamine biosynthesis III
Karatan05: Karatan E, Duncan TR, Watnick PI (2005). "NspS, a predicted polyamine sensor, mediates activation of Vibrio cholerae biofilm formation by norspermidine." J Bacteriol 187(21);7434-43. PMID: 16237027
Lee09: Lee J, Sperandio V, Frantz DE, Longgood J, Camilli A, Phillips MA, Michael AJ (2009). "An alternative polyamine biosynthetic pathway is widespread in bacteria and essential for biofilm formation in Vibrio cholerae." J Biol Chem 284(15);9899-907. PMID: 19196710
Shaw10: Shaw FL, Elliott KA, Kinch LN, Fuell C, Phillips MA, Michael AJ (2010). "Evolution and multifarious horizontal transfer of an alternative biosynthetic pathway for the alternative polyamine sym-homospermidine." J Biol Chem 285(19);14711-23. PMID: 20194510
Yamamoto86: Yamamoto S, Hamanaka K, Suemoto Y, Ono B, Shinoda S (1986). "Evidence for the presence of a novel biosynthetic pathway for norspermidine in Vibrio." Can J Microbiol 32(2);99-103. PMID: 3697846
Alvarez04: Alvarez E, Ramon F, Magan C, Diez E (2004). "L-cystine inhibits aspartate-beta-semialdehyde dehydrogenase by covalently binding to the essential 135Cys of the enzyme." Biochim Biophys Acta 1696(1);23-9. PMID: 14726201
Angeles90: Angeles TS, Viola RE (1990). "The kinetic mechanisms of the bifunctional enzyme aspartokinase-homoserine dehydrogenase I from Escherichia coli." Arch Biochem Biophys 283(1);96-101. PMID: 2241177
Bearer78b: Bearer CF, Neet KE (1978). "Threonine inhibition of the aspartokinase--homoserine dehydrogenase I of Escherichia coli. A slow transient and cooperativity of inhibition of the aspartokinase activity." Biochemistry 1978;17(17);3523-30. PMID: 28752
Biellmann80a: Biellmann JF, Eid P, Hirth C (1980). "Affinity labeling of the Escherichia coli aspartate-beta-semialdehyde dehydrogenase with an alkylating coenzyme analogue. Half-site reactivity and competition with the substrate alkylating analogue." Eur J Biochem 1980;104(1);65-9. PMID: 6102911
Blanco03: Blanco J, Moore RA, Kabaleeswaran V, Viola RE (2003). "A structural basis for the mechanism of aspartate-beta-semialdehyde dehydrogenase from Vibrio cholerae." Protein Sci 12(1);27-33. PMID: 12493825
Broglie83: Broglie KE, Takahashi M (1983). "Fluorescence studies of threonine-promoted conformational transitions in aspartokinase I using the substrate analogue 2'(3')-O-(2,4,6-trinitrophenyl)adenosine 5'-triphosphate." J Biol Chem 1983;258(21);12940-6. PMID: 6313682
Canovas98: Canovas D, Vargas C, Calderon MI, Ventosa A, Nieto JJ (1998). "Characterization of the genes for the biosynthesis of the compatible solute ectoine in the moderately halophilic bacterium Halomonas elongata DSM 3043." Syst Appl Microbiol 1998;21(4);487-97. PMID: 9924816
Chen93b: Chen NY, Jiang SQ, Klein DA, Paulus H (1993). "Organization and nucleotide sequence of the Bacillus subtilis diaminopimelate operon, a cluster of genes encoding the first three enzymes of diaminopimelate synthesis and dipicolinate synthase." J Biol Chem 268(13);9448-65. PMID: 8098035
FalcozKelly69: Falcoz-Kelly F, van Rapenbusch R, Cohen GN (1969). "The methionine-repressible homoserine dehydrogenase and aspartokinase activities of Escherichia coli K 12. Preparation of the homogeneous protein catalyzing the two activities. Molecular weight of the native enzyme and of its subunits." Eur J Biochem 8(1);146-52. PMID: 4889171
Ikai97: Ikai H, Yamamoto S (1997). "Identification and analysis of a gene encoding L-2,4-diaminobutyrate:2-ketoglutarate 4-aminotransferase involved in the 1,3-diaminopropane production pathway in Acinetobacter baumannii." J Bacteriol 179(16);5118-25. PMID: 9260954
James02: James CL, Viola RE (2002). "Production and characterization of bifunctional enzymes. Domain swapping to produce new bifunctional enzymes in the aspartate pathway." Biochemistry 41(11);3720-5. PMID: 11888289
Jullien88: Jullien M, Baudet S, Rodier F, Le Bras G (1988). "Allosteric transition of aspartokinase I-homoserine dehydrogenase I studied by time-resolved fluorescence." Biochimie 1988;70(12);1807-14. PMID: 3150686
Kalinowski91: Kalinowski J, Cremer J, Bachmann B, Eggeling L, Sahm H, Puhler A (1991). "Genetic and biochemical analysis of the aspartokinase from Corynebacterium glutamicum." Mol Microbiol 5(5);1197-204. PMID: 1956296
Showing only 20 references. To show more, press the button "Show all references".
©2015 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493