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            -Glyceraldehyde 3-Phosphate, a Bactericidal Agent

Tang, Chu-Tay; Engel, Robert; Tropp, Burton E.

doi:10.1128/aac.11.1.147

Cited by 20 publications

(22 citation statements)

References 20 publications

(10 reference statements)

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“…Intracellular L-GAP can also be formed by a glycerokinase-catalyzed phosphorylation of L-glyceraldehyde that is taken up from the growth medium (12). The mechanism by which L-GAP causes E. coli to lose viability is not known.…”

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confidence: 99%

“…Since the hydrated form may be considered an analog of sn-G3P, L-GAP has the potential to interfere with enzymes involved in sn-G3P metabolism. L-GAP is a competitive inhibitor of both sn-G3P acyltransferase and phosphatidylglycerol phosphate synthetase (12,13). However, these inhibitory activities do not necessarily explain the bactericidal activity of L-GAP.…”

mentioning

confidence: 99%

“…Cell-free bacterial extracts catalyzed an NADPH-dependent reduction of L-GAP to sn-G3P. The partially purified enzyme was specific for L-GAP and recognized neither D-GAP nor (5,12). Intracellular L-GAP can also be formed by a glycerokinase-catalyzed phosphorylation of L-glyceraldehyde that is taken up from the growth medium (12).…”

mentioning

confidence: 99%

“…L-Glyceraldehyde 3-phosphate (GAP) is a bactericidal agent that enters Escherichia coli via either the sn-glycerol 3-phosphate (G3P) or hexose phosphate transport system (5,12). Intracellular L-GAP can also be formed by a glycerokinase-catalyzed phosphorylation of L-glyceraldehyde that is taken up from the growth medium (12).…”

mentioning

confidence: 99%

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Metabolism of L-glyceraldehyde 3-phosphate in Escherichia coli

Kalyananda¹,

Engel²,

Tropp³

1987

J Bacteriol

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When either 3H-labeled L-glyceraldehyde or 3H-labeled L-glyceraldehyde 3-phosphate (GAP) was added to cultures of Escherichia coli, the phosphoglycerides were labeled. More than 81% of the label appeared in the backbone of the phosphoglycerides. Chromatographic analyses of the labeled phosphoglycerides revealed that the label was normally distributed into phosphatidylethanolamine, phosphatidylglycerol, and cardiolipin. These results suggest that L-glyceraldehyde is phosphorylated and the resultant L-GAP is converted into sn-glycerol 3-phosphate (G3P) before being incorporated into the bacterial phosphoglycerides. Cell-free bacterial extracts catalyzed an NADPH-dependent reduction of L-GAP to sn-G3P. The partially purified enzyme was specific for L-GAP and recognized neither D-GAP nor (5,12). Intracellular L-GAP can also be formed by a glycerokinase-catalyzed phosphorylation of L-glyceraldehyde that is taken up from the growth medium (12). The mechanism by which L-GAP causes E. coli to lose viability is not known.One possibility is that L-GAP exerts its bactericidal effect by interfering with a critical biochemical reaction. In aqueous solution, L-GAP exists as an equilibrium mixture of the hydrated and free aldehyde in a molar ratio of 29:1 (14). Since the hydrated form may be considered an analog of sn-G3P, L-GAP has the potential to interfere with enzymes involved in sn-G3P metabolism. L-GAP is a competitive inhibitor of both sn-G3P acyltransferase and phosphatidylglycerol phosphate synthetase (12, 13). However, these inhibitory activities do not necessarily explain the bactericidal activity of L-GAP. The sn-G3P analogs 3-hydroxy-4-oxobutyl-1-phosphonate and 1,3,4-trihydroxybutyl-1-phosphonate are bacteriostatic rather than bactericidal, even though they also inhibit the two lipid enzymes (13; unpublished

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confidence: 99%

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confidence: 99%

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confidence: 99%

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Metabolism of L-glyceraldehyde 3-phosphate in Escherichia coli

Kalyananda¹,

Engel²,

Tropp³

1987

J Bacteriol

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“…Effect of respiratory condition of growth on the ability of wild-type strain ECL1 to retain the aldehyde or methyl end of L-fucose. Cells were assayed for retention of radioactivity after incubation with L-fucose labeled at C-1 (*) or C-6 (0) as described in Materials and Methods, (A) Aerobic growth on L-fucose (high aldehyde dehydrogenase specific activity and low L-1,2-propanediol specific activity [12]); (B) anaerobic growth on L-fucose (low aldehyde dehydrogenase specific activity and high L-1,2-propanediol oxidoreductase activity [12] (25).…”

Section: Discussionmentioning

confidence: 99%

Loss of aldehyde dehydrogenase in an Escherichia coli mutant selected for growth on the rare sugar L-galactose

Zhu¹,

Lin²

1987

J Bacteriol

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Escherichia coli K-12 converts L-fucose to dihydroxyacetone phosphate (C-1 to C-3) and L-lactaldehyde (C-4 to C-6) by a pathway specified by thefuc regulon. Aerobically, L-lactaldehyde serves as a carbon and energy source by the action of an aldehyde dehydrogenase of broad specificity; the product, L-lactate, is then converted to pyruvate. Anaerobically, L-lactaldehyde serves as an electron acceptor to regenerate NAD from NADH by the action of an oxidoreductase; the reduced product, L-1,2-propanediol, is excreted. A strain selected for growth on L-galactose (a structural analog of L-fucose) acquired a broadened inducer specificity because of an altered fucR gene encoding the activator protein for the fuc regulon (Y. Zhu and E. C. C. Lin, J. Mol. Evol. 23:259-266, 1986). In this study, a second mutation that abolished aldehyde dehydrogenase activity was discovered. The L-fucose pathway converts L-galactose to dihydroxyacetone phosphate and L-glyceraldehyde. Aldehyde dehydrogenase then converts L-glyceraldehyde to L-glycerate, which is toxic. Loss of the dehydrogenase averts the toxicity during growth on L-galactose, but reduces by one-half the aerobic growth yield on L-fucose. When mutant cells induced in the L-fucose system were incubated with radioactive L-fucose, accumulation of radioactivity occurred if the substrate was labeled at C-1 but not if it was labeled C-6. Complete aerobic utilization of carbons 4 through 6 of L-fucose depends not only on an adequate activity of aldehyde dehydrogenase to trap L-lactaldehyde as its anionic acid but also on the lack of L-1,2-propanediol oxidoreductase activity, which converts L-lactaldehyde to a readily excreted alcohol.Escherichia coli K-12 grows on L-fucose as the sole carbon and energy source via an inducible pathway mediated by the sequential action of L-fucose permease (12), L-fucose isomerase (10), L-fuculose kinase (14), and L-fuculose 1-phosphate aldolase (9). The aldolase cleaves the six-carbon substrate into dihydroxyacetone phosphate and Llactaldehyde. Aerobically, L-lactaldehyde is oxidized by an NAD-linked dehydrogenase to L-lactate, which is converted to pyruvate by a dehydrogenase of the flavoprotein class. Anaerobically, L-lactaldehyde is reduced by an NADHlinked oxidoreductase to L-1,2-propanediol, which is then excreted (7,22,23). The sacrifice of one-half of the carbon skeleton of L-fucose permits more dihydroxyacetone phosphate to be used as a carbon source (Fig. 1). The structural genes fucP (encoding the permease), fucI (encoding the isomerase), fucK (encoding the kinase), fucA (encoding the aldolase), andfucO (encoding L-1,2-propanediol oxidoreductase) are organized into three operons clustered at min 60.2 (3,5,6,(11)(12)(13) tor gene altered the inducer specificity in such a way that the fuc regulon became triply inducible by L-galactose, D-arabinose, or L-fucose. However, it was noticed that growth of the mutant on L-fucose agar gave colonies of subnormal size. Moreover, the introduction of fucR+ on a multicopy plasmid diminished growth on L-...

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Straightforward Synthesis of Terminally Phosphorylated L‐Sugars via Multienzymatic Cascade Reactions

et al. 2015

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Tw ok inases and the key fructose-6-phosphate aldolase (FSA) were involved in ao ne-pot multienzymatic procedure to obtain rare l-sugars. Starting from simplea chiral substrates such as glycolaldehyde andf ormaldehyde, l-glyceraldehyde-3phosphate( l -G3P) was generated. When this latter compound was used as an FSA acceptor substrate along with four different donor compounds,f our terminally phosphorylated l-monosaccharides from C 5 to C 7 chain lengths were preparedi ng oodi solated yields.

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l -Glyceraldehyde 3-Phosphate, a Bactericidal Agent

Cited by 20 publications

References 20 publications

Metabolism of L-glyceraldehyde 3-phosphate in Escherichia coli

Metabolism of L-glyceraldehyde 3-phosphate in Escherichia coli

Loss of aldehyde dehydrogenase in an Escherichia coli mutant selected for growth on the rare sugar L-galactose

Straightforward Synthesis of Terminally Phosphorylated L‐Sugars via Multienzymatic Cascade Reactions

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