Fructose-bisphosphate aldolases: an evolutionary history

Marsh, James J.; Lebherz, Herbert G.

doi:10.1016/0968-0004(92)90247-7

Cited by 209 publications

(167 citation statements)

References 22 publications

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“…Two classes of this enzyme, designated Class I and Class II, are recognised based on their catalytic and structural properties [ 1,2]. The catalytic mechanism of the Class I aldolases has been extensively studied [3,4].…”

Section: Introductionmentioning

confidence: 99%

Identification of zinc‐binding ligands in the Class II fructose‐ 1,6‐bisphosphate aldolase of Escherichia coli

Berry

Marshall

1993

FEBS Letters

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An expression and mutagenesis system for the E. coli Class II fructose-l ,6-bisphosphate aldolase has been created by modification of the vector pKfda (B&hem. J. 257 (1989) 529-534). Large amounts of Class II aldolase (about 1 g/l in crude extracts), with properties consistent with those previously reported for the naturally occurring enzyme (B&hem. J. 169 (1978) 6333641) are obtained. The enzyme contains 2 zinc ions per enzyme dimer. We have investigated the nature of the zinc-binding site of the enzyme by site-directed mutagenesis. His-108, His-l 11, were identified as possible zinc-binding ligands by sequence alignments and comparisons with other known zinc-containing enzymes. Mutation of these residues identified His-108 and His-l 11 as two of the ligands directly responsible for the tight binding of zinc. Mutation of the other two residues results in only a small effect on the amount of zinc bound per monomer and a corresponding change in specific activity. These residues are, therefore, unlikely to be directly involved in zinc binding, but may be indirectly involved in some manner in the zinc-binding environment.

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Section: Introductionmentioning

confidence: 99%

Identification of zinc‐binding ligands in the Class II fructose‐ 1,6‐bisphosphate aldolase of Escherichia coli

Berry

Marshall

1993

FEBS Letters

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“…They are mainly found in lower organisms such as bacteria (eubacteria and archeabacteria), fungi, protozoa, and some green algae. Class I and class II enzymes show almost no sequence similarities and are assumed to have arisen from separate evolutionary origins (20). The absence of class II FBAs from mammalian cells and the specificity of their structure and catalytic mechanism thus offer the opportunity to design drugs that selectively inhibit microbial class II enzymes without affecting the gluconeogenetic and glycolytic pathways of the host.…”

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confidence: 99%

Glycolytic and Non-glycolytic Functions of Mycobacterium tuberculosis Fructose-1,6-bisphosphate Aldolase, an Essential Enzyme Produced by Replicating and Non-replicating Bacilli

Santangelo

Gest

Guerin

et al. 2011

Journal of Biological Chemistry

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Background: New drugs active against persistent Mycobacterium tuberculosis are needed. Results: The fructose-1,6-bisphosphate aldolase (FBA-tb) is essential for growth of M. tuberculosis, is expressed by replicating and non-replicating bacilli, and displays plasminogen binding activity. Conclusion: FBA-tb is an essential TB enzyme that might also play a role in host/pathogen interactions. Significance: FBA-tb shows potential as a novel anti-TB therapeutic target.

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“…As one of the reasons for this glucose pattern, we have discussed isotope effects on several reactions of the pentose phosphate cycle, especially on the fructose-1,6-bisphosphate aldolase reaction. In order to verify this assumption we have now determined the kinetic and the equilibrium isotope effects on this reaction.We used for our experiments the well characterized Class I rabbit muscle aldolase (18,19), which belongs to the same class as the cytosolic plant enzyme (20,21). Rabbit muscle aldolase is a homotetramer with a molecular mass of 160 kDa, each subunit occurring in an ␣/␤ barrel (22).…”

mentioning

confidence: 99%

“…We used for our experiments the well characterized Class I rabbit muscle aldolase (18,19), which belongs to the same class as the cytosolic plant enzyme (20,21). Rabbit muscle aldolase is a homotetramer with a molecular mass of 160 kDa, each subunit occurring in an ␣/␤ barrel (22).…”

mentioning

confidence: 99%

Carbon Isotope Effects on the Fructose-1,6-bisphosphate Aldolase Reaction, Origin for Non-statistical 13C Distributions in Carbohydrates

Gleixner

Schmidt

1997

Journal of Biological Chemistry

120

107

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The kinetic and equilibrium isotope effects on the fructose-1,6-bisphosphate aldolase reaction have been determined using the rabbit muscle enzyme. The natural 13 C abundance for both atoms participating in the bond splitting were measured in position C-1 of dihydroxyacetone phosphate and glyceraldehyde 3-P after irreversible conversion to glycerol-3-P and 3-phosphoglycerate, respectively, and chemical degradation. The carbon isotope effects were determined comparing the 13 C content of the corresponding positions after partial and complete turnover, and after complete equilibration of the reactants. 13 (V max /K m ) on C-3 was 1.016 ؎ 0.007 and 0.997 ؎ 0.009 on position C-4, and the equilibrium isotope effects K 12 /K 13 on these positions were 1.0036 ؎ 0.0002 and 1.0049 ؎ 0.0001.The observed kinetic isotope effect on C-3 is discussed to originate from the formation of the enamine, which comes to equilibrium before the rate determining release of glyceraldehyde 3-P from the ternary complex. The equilibrium isotope effect is seen as the reason for an earlier-found relative 13 C enrichment in position C-3 and C-4 of glucose and for varying enrichments in 13 C of carbohydrates from different compartments of cells. The kinetic isotope effect is suggested to cause 13 C discriminations in the C-3 pool in context with the hexose formation in competition with other dihydroxyacetone phosphate turnover reactions.The relative enrichment of carbon-13 in the carboxyl group of amino acids, as observed by Abelson and Hoering (1) in 1961, was the first indication for the existence of non-statistical isotope distributions in biological compounds. Later results on acetic acid (2) and on acetoin (3) gave evidence that this observation was just one example of a common phenomenon. In order to find a general explanation for this observation Galimov (4) discussed that even in chemically unequilibrated systems, e.g. biological systems, a microscopic reversibility in enzymatic reactions is the origin for a thermodynamically ordered isotope distribution. The author's calculations could in fact explain some of the isotopic patterns of natural compounds known at that time. However, the presumption of a general thermodynamic equilibrium in biological systems is probably not realistic. In our opinion kinetic isotope effects on enzymatic reactions should be considered as primary causes for isotope discriminations. This has been proven for the primary CO 2 -fixing reactions (5-8). In secondary metabolism, the isotope effect on the pyruvate dehydrogenase reaction has been made responsible for the general depletion of 13 C in metabolites of acetyl-CoA, such as fatty acids or isoprenoids (9 -15).More detailed interpretations were possible when the total isotopic patterns of primary and secondary metabolites became available. Especially, our corresponding investigations on glucose indicated an enrichment of 13 C in positions C-3 and C-4, and a depletion of 13 C in positions C-1 and C-6 (Fig. 1) of this important primary metabolite (16). We have a...

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Fructose-bisphosphate aldolases: an evolutionary history

Cited by 209 publications

References 22 publications

Identification of zinc‐binding ligands in the Class II fructose‐ 1,6‐bisphosphate aldolase of Escherichia coli

Identification of zinc‐binding ligands in the Class II fructose‐ 1,6‐bisphosphate aldolase of Escherichia coli

Glycolytic and Non-glycolytic Functions of Mycobacterium tuberculosis Fructose-1,6-bisphosphate Aldolase, an Essential Enzyme Produced by Replicating and Non-replicating Bacilli

Carbon Isotope Effects on the Fructose-1,6-bisphosphate Aldolase Reaction, Origin for Non-statistical 13C Distributions in Carbohydrates

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