Novel kinetic and structural properties of the class-I <scp>D</scp>-fructose 1,6-bisphosphate aldolase from <i>Escherichia coli</i> (Crookes' strain)

Baldwin, S. A.; Perham, Richard N.

doi:10.1042/bj1690643

Cited by 46 publications

(28 citation statements)

References 24 publications

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“…The molecular masses for L. casei aldolase reported from various 1abOrdtOrieS do not agree [ S , 61. The class 1 aldolase from E. coli was reported to be a decainer of340 kDa [8] but a later report from another laboratory reported 1321 that it 'eluted at the same place as the rabbit muscle aldolase on Sephadex G-150'. More recently, the occurrence of class I aldolase of molecular mass around Except for these monomeric aldolases, class I aldolases, including the non-Fru(3 ,6)P2 aldolases, are known to be oligomeric molecules [33,341.…”

Section: Discussionmentioning

confidence: 99%

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An unusual class I (Schiff base) fructose‐1,6‐bisphosphate aldolase from the halophilic archaebacterium Haloarcula vallismortis

Krishnan

Altekar

1991

European Journal of Biochemistry

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An electrophoretically homogeneous class I (Schiff base) alsolase has been isolated for the first time from the archaebacterial halophile Haloarcula (Halobacterium) vallismortis. The aldolase was characterized with respect to its molecular mass, amino acid composition, salt dependency, immunological cross-reactivity and kinetic properties. The subunit mass of aldolase is 27 kDa, which is much smaller than other class I aldolases. By the gel filtration method, the molecular mass of the halobacterial enzyme was estimated as 280 k 10 kDa, suggesting a decameric nature. In contrast to many halobacterial proteins, the H . vallismortis aldolase, though a halophilic enzyme, did not show an excess of acidic residues. Unlike the eukaryotic aldolases, the activity of the halobacterial enzyme was not affected by carboxypeptidase digestion. The general catalytic features of the enzyme were similar to its counterparts from other sources. No antigenic similarity could be detected between the H. vallisrnortis aldolase and class I aldolase from eubacteria and eukaryotes or class I1 halobacterial aldolases.Two types of fructose-l,6-bisphosphate [Fru(l,6)Pz] aldolases, viz. class I and class 11, are known. Aldolases from most microorganisms show the characteristics of class 11 and are metalloenzymes [l]. Thus, class I1 aldolases are inhibited by EDTA as they are dependent on a divalent metal ion for the stabilization of the carbanion intermediate of the aldolasesubstrate complex [l]. In contrast, the class I aldolases distributed in higher forms of life, such as animals, protozoa, algae and higher plants, form a Schiff base intermediate involving the e-NH, group of a lysine residue and glycerone phosphate (GrnP) [2]. This Schiff base can be reduced with NaBH4, thereby inactivating the enzyme irreversibly [2].From the information then available on the restrictive phylogenetic segregation of aldolases in nature, it was considered that the gene for class I aldolase appeared later than that for the class I1 enzyme [l]. Therefore the identification of class I aldolases in certain eubacteria came as a surprise. These bacteria were : Micrococcus aerogenes [3,4], Lactobacillus casei [5, 61, Mycobacterium smegmatis [7], Escherichia coli [8], Staphylococcus aureus [9] and species of Staphylococci and Peptococci [lo]. The amino acid sequences near the active site reported for M . aerogenes [4] and S. aureus [ll] were shown to exhibit 48% and 21 YO similarity, respectively, with the mammalian aldolases. Recently our work on halobacterial aldolases has added the name of archaebacterial halophiles to this list of unusual class I aldolases in prokaryotes [12, 131.

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Section: Discussionmentioning

confidence: 99%

“…Therefore the identification of class I aldolases in certain eubacteria came as a surprise. These bacteria were : Micrococcus aerogenes [3,4], Lactobacillus casei [5, 61, Mycobacterium smegmatis [7], Escherichia coli [8], Staphylococcus aureus [9] and species of Staphylococci and Peptococci [lo]. The amino acid sequences near the active site reported for M .…”

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confidence: 99%

An unusual class I (Schiff base) fructose‐1,6‐bisphosphate aldolase from the halophilic archaebacterium Haloarcula vallismortis

Krishnan

Altekar

1991

European Journal of Biochemistry

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“…Evidently this enzyme is not induced or is of insufficient activity to allow growth offda mutants on hexoses. The two E. coli aldolases were found subject to metabolic effectors (115,120). In E. coli the aldolase reaction is not at equilibrium in vivo, for C-b from glucose did not label equally the 1-and 6-positions of fructose-l,6-P2 (121,122).…”

Section: Phosphofructokinase and Fructose Bisphosphatasementioning

confidence: 95%

“…Re sidual aldolase activity in the mutants might depend on a second aldolase, and a type 1 aldolase has been described in the Crookes' strain of E. coli (120). Evidently this enzyme is not induced or is of insufficient activity to allow growth offda mutants on hexoses.…”

Section: Phosphofructokinase and Fructose Bisphosphatasementioning

confidence: 97%

Mutants in Glucose Metabolism

Fraenkel¹

1986

Annu. Rev. Biochem.

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“…For example, the mutant subunit could have a higher affinity for wild-type than mutant enzyme, leading to many more mixed dimers than expected on statistical grounds, or may be able to associate with other aldolase subunits following partial denaturation, thus permitting it to catalyze the denaturation of many of the remaining wild-type subunits. Alternatively, Fda might act as a tetramer in vivo, although it has been reported to sediment as a dimer in vitro (5,6,31). The low amount of wild-type aldolase activity that we observed in the mutant/wild-type merodiploid would be expected if Fda were a tetramer and a single mutant Fda monomer was able to poison the tetramer.…”

Section: Resultsmentioning

confidence: 49%

The Escherichia coli ts8 mutation is an allele of fda, the gene encoding fructose-1,6-diphosphate aldolase

et al. 1991

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The ts8 mutant of Escherichia coli has previously been shown to preferentially inhibit stable RNA synthesis when shifted to the nonpermissive temperature. We demonstrate in this report that the ts8 mutation is an allele offda, the gene that encodes the glycolytic enzyme fructose-1,6-diphosphate aldolase. We show that ts8 and a secondfda mutation, h8, isolated and characterized by A. Bock and F. C. Neidhardt, are dominant mutations and that they encode a thermolabile aldolase activity.The rate of protein synthesis in Escherichia coli is proportional to the number of ribosomes within the normal range of growth rates, suggesting that ribosomes are utilized at a constant efficiency. In order for cells to grow twice as fast, they must make twice as many ribosomes in half the time. This is reflected in the fact that the rate of ribosome synthesis varies with the square of the growth rate (,U2) (19). Because the rate of rRNA synthesis controls the rate of ribosome synthesis, the cell must have a mechanism for adjusting the rate of rRNA synthesis to the growth rate. Although the system of growth rate control has been studied intensively, the regulators responsible for this response are still unknown.One approach to studying the regulation of stable RNA synthesis is to isolate and characterize mutations that preferentially affect RNA expression. One class of mutants that meet this criteria are those defective in producing ppGpp, a molecule believed to preferentially inhibit the synthesis of stable RNA. Amino acid starvation triggers the accumulation of ppGpp, leading to a preferential decrease in the rate of stable RNA synthesis and has been termed the stringent response (28). relA and spoT strains are defective in this response. The ts8 mutation of Liebke and Speyer (17) represents a second class of mutations that preferentially affects the expression of stable RNA. Strains carrying the ts8 mutation have been shown to preferentially inhibit stable RNA synthesis after a shift to a nonpermissive temperature. In this report, we examine the genetic basis for this mutation and show that ts8 is an allele offda, the gene that encodes the glycolytic enzyme fructose-1,6-diphosphate aldolase (Fda). In addition, we show that another strain containing a different mutation infda, h8, isolated by Bock and Neidhardt (8,9), behaves similarly to ts8. The accompanying report (27) presents a detailed characterization of the effect of ts8 on the capacity of the cell to synthesize rRNA. MATERIALS AND METHODSStrains and growth conditions. All strains used were E. coli K-12 Genetic manipulations. P1 transductions and F' matings were performed as described by Miller (21); transductions using T4GT7 were done as described by Young and Edlin (33). The ts8 allele was transferred into strain CAG12516 by T4-mediated transduction. The resulting strain, CAG12513, was used for all further genetic and physiological characterizations unless indicated otherwise. All mapping assays were performed by mapping the temperature-sensitive (Ts) phenotype, by s...

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Novel kinetic and structural properties of the class-I D-fructose 1,6-bisphosphate aldolase from Escherichia coli (Crookes' strain)

Cited by 46 publications

References 24 publications

An unusual class I (Schiff base) fructose‐1,6‐bisphosphate aldolase from the halophilic archaebacterium Haloarcula vallismortis

An unusual class I (Schiff base) fructose‐1,6‐bisphosphate aldolase from the halophilic archaebacterium Haloarcula vallismortis

Mutants in Glucose Metabolism

The Escherichia coli ts8 mutation is an allele of fda, the gene encoding fructose-1,6-diphosphate aldolase

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