Paracatalytic self‐inactivation of fructose‐1,6‐bisphosphate aldolase

Gupta, Sharad; Hollenstein, Roger; Kochhar, Sunil; Christen, Philipp

doi:10.1111/j.1432-1033.1993.tb17949.x

Cited by 13 publications

(12 citation statements)

References 15 publications

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“…In contrast, addition of water (3) and lysine (4) at the imine moiety initiates formation of GALA and GLA, respectively. While amides GALA and GOLA were already established to be part of this CML-isomerization cascade not only in model reactions but also in foods and in vivo , amidine formation is so far not known in the Maillard chemistry field. ,, Amidine lysine cross-link formation was proposed by Gupta et al to occur during self-inactivation of fructose-1,6-bisphosphate aldolase via a 1,2-hydride shift of a geminal diamine intermediate . Interestingly, the glyoxal-derived imidazoline cross-link (GODIC) was proposed by Lederer and Klaiber to be formed by the reaction of glyoxal-imines with arginine via a geminal diamine through a similar intramolecular redox process .…”

Section: Resultsmentioning

confidence: 99%

Novel Amidine Protein Cross-Links Formed by the Reaction of Glyoxal with Lysine

Eggen

Glomb

2021

J. Agric. Food Chem.

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One crucial aspect of the Maillard reaction is the formation of reactive α-dicarbonyl structures like glyoxal, which are prone toward further reactions with proteins, e.g., the N6 -amino group of lysine. The initially formed labile glyoxal-imine was previously established as a key intermediate in the formation of the advanced glycation end products N 6-carboxymethyl lysine (CML), glyoxal lysine amide (GOLA), glyoxal lysine dimer (GOLD), and N 6-glycolyl lysine (GALA). Here, we introduce a novel amidine cross-link structure N 1,N 2-bis-(5-amino-5-carboxypentyl)-2-hydroxy-acetamidine (glyoxal lysine amidine, GLA), which is formed exclusively from glyoxal through the same isomerization cascade. After independent synthesis of the authentic reference standard, we were able to quantitate this cross-link in incubations of 40 mM N 2-t-Boc-lysine with glyoxal and various sugars (40–100 mM) under mild conditions (pH 7.4, 37 °C) using an HPLC–MS/MS method. Furthermore, incubations of proteins (6 mg/mL) with 50 mM glyoxal confirmed the cross-linking by GLA, which was additionally identified in acidic hydrolyzed proteins of butter biscuits after HPLC enrichment.

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Section: Resultsmentioning

confidence: 99%

Novel Amidine Protein Cross-Links Formed by the Reaction of Glyoxal with Lysine

Eggen

Glomb

2021

J. Agric. Food Chem.

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“…Oxidants (e.g. ferricyanide) also cause self-inactivation of aldolase [37]. Aldolase, like NADH dehydrogenases, binds NADH with high affinity (K D 6n0i10 −' ), inducing strong conformational changes [38].…”

Section: Discussionmentioning

confidence: 99%

Purification of a dichlorophenol-indophenol oxidoreductase from rat and bovine synaptic membranes: tight complex association of a glyceraldehyde-3-phosphate dehydrogenase isoform, TOAD64, enolase-γ and aldolase C

Bulliard

Zurbriggen

Tornare

et al. 1997

Biochemical Journal

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NADH-dichlorophenol-indophenol oxidoreductases (PMOs) were purified from synaptic plasma membranes or synaptic vesicles (small recycling vesicles) from both bovine and rat brains and from a neuroblastoma cell line, NB41A3. Several isoforms could be identified in purified plasma membranes and vesicles. Purification of the enzyme activity involved protein extraction with detergents, (NH4)2SO4 precipitation, chromatography under stringent conditions and native PAGE. PMO activity could be attributed to a very tight complex of several proteins that could not be separated except by SDS/PAGE. SDS/PAGE resolved the purified complex into at least five proteins, which could be micro-sequenced and identified unambiguously as hsc70, TOAD64 and glyceraldehyde-3-phosphate dehydrogenase tightly associated with the brain-specific proteins aldolase C and enolase-gamma. Enzyme activity could be purified from both synaptic plasma membranes and recycling vesicles, yields being much greater from the latter source. Highly purified plasma membranes (prepared from a neuroblastoma cell line NB41A3 by iminobiotinylation of intact cells and affinity purification with avidin and anti-avidin antibodies under very stringent conditions) also displayed PMO activity tightly associated with TOAD64. The association of PMO in a tight complex was confirmed by its immunoprecipitation from cellular and membrane extracts of NB41A3 using antibodies directed against any component protein of the complex followed by immunodetection with antibodies directed against the other members. Antibodies also inhibited the enzyme activity synergistically. In addition, induction of the different components of the complex during dichlorophenol-indophenol stress was demonstrated by the S1 RNase-protection assay in synchronized NB41A3 cells. The role of the complex in membrane fusion and cellular response to extracellular oxidative stress during growth and development is discussed.

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“…At this point, amidine formation within Maillard reaction chemistry was unknown. However, studies on the paracatalytic self-inactivation of fructose-1,6-bisphosphate aldolase by oxidants provided structural evidence of amidine formation (28). As shown in the scheme in Fig.…”

Section: Fig 2 Verification Of Gola In Ribose/n ␣ -T-boc-lysine Incmentioning

confidence: 99%

Amides Are Novel Protein Modifications Formed by Physiological Sugars

Glomb

Pfahler

2001

Journal of Biological Chemistry

129

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The Maillard reaction, or nonenzymatic browning, proceeds in vivo, and the resulting protein modifications (advanced glycation end products) have been associated with various pathologies. Despite intensive research only very few structures have been established in vivo. We report here for the first time N 6 -{2-[(5-amino-5-carboxypentyl)amino]-2-oxoethyl}lysine (GOLA) and N 6 -glycoloyllysine (GALA) as prototypes for novel amide protein modifications produced by reducing sugars. Their identity was confirmed by independent synthesis and coupled liquid chromatography/mass spectrometry. Model reactions with N ␣ -t-butoxycarbonyl-lysine showed that glyoxal and glycolaldehyde are immediate precursors, and reaction pathways are directly linked to N ⑀ -carboxymethyllysine via glyoxal-imine structures. GOLA, the amide cross-link, and 1,3-bis(5-amino-5-carboxypentyl)imidazolium salt (GOLD), the imidazolium cross-link, share a common intermediate. The ratio of GOLA to GOLD is greater when glyoxal levels are low at constant lysine concentrations. GOLA and GALA formation from the Amadori product of glucose and lysine depends directly upon oxidation. With the advanced glycation end product inhibitors aminoguanidine and pyridoxamine we were able to dissect oxidative fragmentation of the Amadori product as a second mechanism of GOLA formation exactly coinciding with N ⑀ -carboxymethyllysine synthesis. In contrast, the formation of GALA appears to depend solely upon glyoxal-imines. After enzymatic hydrolysis GOLA was found at 66 pmol/mg of brunescent lens protein. This suggests amide protein modifications as important markers of pathophysiological processes.

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Paracatalytic self‐inactivation of fructose‐1,6‐bisphosphate aldolase

Cited by 13 publications

References 15 publications

Novel Amidine Protein Cross-Links Formed by the Reaction of Glyoxal with Lysine

Novel Amidine Protein Cross-Links Formed by the Reaction of Glyoxal with Lysine

Purification of a dichlorophenol-indophenol oxidoreductase from rat and bovine synaptic membranes: tight complex association of a glyceraldehyde-3-phosphate dehydrogenase isoform, TOAD64, enolase-γ and aldolase C

Amides Are Novel Protein Modifications Formed by Physiological Sugars

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