Fructose-1,6-bisphosphate aldolase from Drosophila melanogaster: Primary structure analysis, secondary structure prediction, and comparison with vertebrate aldolases

Malek, Antoine A.; Hy, Malene; Honegger, Annemarie; Rose, Keith; Brenner‐Holzach, O.

doi:10.1016/0003-9861(88)90232-9

Cited by 22 publications

(22 citation statements)

References 43 publications

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“…There the sequence differs considerably [4]: in DALD residue 239 is missing and residues 240-243 are AIa, Lys, Lys, Asn. For RMALD the sequence for residues 239-243 is Cys, Thr, Gln, Lys, Tyr.…”

Section: Resultsmentioning

confidence: 99%

“…Each subunit of the insect enzyme consists of 360 amino acids. The primary structure of DALD is reported in [4]. Compared to vertebrate aldolases the insect enzyme shows 62-70% identical amino acids [4].…”

Section: Intrc Ductionmentioning

confidence: 99%

“…The primary structure of DALD is reported in [4]. Compared to vertebrate aldolases the insect enzyme shows 62-70% identical amino acids [4]. Based on biochemical properties and primary sequence alignments it was suggested [4] that DALD is closest to the muscle type aldolases of vertebrates.…”

Section: Intrc Ductionmentioning

confidence: 99%

“…Compared to vertebrate aldolases the insect enzyme shows 62-70% identical amino acids [4]. Based on biochemical properties and primary sequence alignments it was suggested [4] that DALD is closest to the muscle type aldolases of vertebrates. DALD is able to form enzymatically active interspecies hybrids with vertebrate aldolases [5].…”

Section: Intrc Ductionmentioning

confidence: 99%

“…In addition, parts of this region in the rabbit muscle aldolase structure are not well determined [7], leaving an uncertainty concerning its conformation. Even though these two known structures were not cornpared to each other the high degree of identity (99%) [4] implies identical tertiary structure [13].…”

Section: *Present Addressmentioning

confidence: 99%

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The crystal structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolution

Hester

Brenner‐Holzach

Rossi³

et al. 1991

FEBS Letters

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The structure of fructose-l,6-bisphosphate aldolase from Drosophila melanogaster has been determined by X-my diffraction at 2.5 .~ resolution.The insect enzyme crystallizes in space group P'2r2~2t with lattice constants a=86.60, b= 116.80, c= 151.58 ~. Molecular replacement with rabbit muscle aldolase as a search model has been employed to solve the structure. To improve the initial phases real space averaging, including phase extension from 4.0 to 2.5 ,/~, has been applied. Refinement of the atomic positions by molecular dynamics resulted in a crystallographic R-factor of 0.214. The tertiary structure resembles in most parts that of the vertebrate aldolase from rabbit muscle. Significant differences were found in surface loops and the N-and C-terminal regions of the protein. Here we present the first aldolase structure where the functionally important C-terminal arm is described completely.Crystal structure; Glycolytic enzyme; Fructose-1,6-bisphosphate aldolase; Substrate specificity; Drosophila melanogaster INTRC, DUCTIONFruetose-l,6-bisphosphate (FBP) aldolase (EC 4.1.2.13) is a glycolytic enzyme catalyzing the reversible aldol cleavage of fructose-l,6-bisphosphate to dihydroxyacetone phosphate and D-glyceraldehyde-3-phosphate. FBP aldolase from Drosophila melanogaster (strain Sevelen, wild type, pupea) forms a Schiff base between the substrate and a lysyl residue [1] and belongs therefore to the class I aldolases [2]. Contrary to class I the class II aldolases use a divalent metal ion as cofactor [3]. The vertebrate aldolases (class I) comprise three isozymes. They refer to A (muscle), B (liver) and C (brain) depending on the tissue from which they are isolated [3]. The A and C form show a higher substrate specificity for FBP over fructose-l-phosphate (F1P), while the liver isozyme has no such preference.Abbreviations: DALD, fructose-l,6-bisphosphate aldolase from Drosophila melanogaster; RMALD, rabbit muscle aldolase; HMALD, human muscle aldolase; RLALD, rabbit liver aldolase; FBP, fructose-1,6-bisphosphate; FIP, fructose-l-phosphate; r.m.s., root-meansquare.Sequence numbering: Throughout this paper the sequence numbering of FBP aldolase from rabbit muscle will be applied.

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Section: Resultsmentioning

confidence: 99%

Section: Intrc Ductionmentioning

confidence: 99%

Section: Intrc Ductionmentioning

confidence: 99%

Section: Intrc Ductionmentioning

confidence: 99%

Section: *Present Addressmentioning

confidence: 99%

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The crystal structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolution

Hester

Brenner‐Holzach

Rossi³

et al. 1991

FEBS Letters

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Formation of CC Bonds: Sections 14.1 ‐ 14.6

Wong¹

2002

Enzyme Catalysis in Organic Synthesis

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The aldol reaction is one of the most powerful methods for carbon-carbon bond formation, and its catalytic asymmetric variants have great potential in contemporary organic synthesis ['I. Aldolases are enzymes which catalyze reversible and irreversible asymmetric aldol condensations in r~ature[~-~], via one of two distinct reaction mechanisms 1 ' 1 . Type I aldolases activate the donor/nucleophilic substrate via Schiff base formation with an active-site lysine residue. These enzymes are predominantly found in animals and higher plants, and do not require metal cofactors. Type I1 aldolases activate both donor and acceptor substrates via chelation to an active-site Zn", and are found mainly in microorganisms. Aldolases can be conveniently classified into groups according to their natural donor substrates, i. e. dihydroxyacetone phosphate (DHAP), pyruvate/phosphoenol pyruvate (PEP), glycine, acetaldehyde, and a small number of other molecules. The ability of aldolases to accept a variety of unnatural acceptor substrates, and to generate new stereocenters of known absolute and relative stereochemistry reliably, has made them powerful tools for asymmetric synthesis.FDP aldolase catalyzes the reversible aldol addition reaction of DHAP and Dglyceraldehyde 3-phosphate (D-G~Y 3-P) to form D-FDP (Fig. 14.1-1). The equilibrium constant for this reaction has a value of -lo4 M-' in favor of FDP formation. The enzyme has been isolated from a variety of eukaryotic and prokaryotic sources, both in type I and type I1 forms [7-211. Generally, the type I FDP aldolases exist as tetramers (M. W. -160 KDa), while the type I1 enzymes are dimers (M. W. -80 KDa). For the

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Formation of CC Bonds

Drauz¹,

Waldmann²

1995

Enzyme Catalysis in Organic Synthesis

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Fructose-1,6-bisphosphate aldolase from Drosophila melanogaster: Primary structure analysis, secondary structure prediction, and comparison with vertebrate aldolases

Cited by 22 publications

References 43 publications

The crystal structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolution

The crystal structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolution

Formation of CC Bonds: Sections 14.1 ‐ 14.6

Formation of CC Bonds

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Fructose-1,6-bisphosphate aldolase from Drosophila melanogaster: Primary structure analysis, secondary structure prediction, and comparison with vertebrate aldolases

Cited by 22 publications

References 43 publications

The crystal structure of fructose&#x2010;1,6&#x2010;bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolution

The crystal structure of fructose&#x2010;1,6&#x2010;bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolution

Formation of CC Bonds: Sections 14.1 ‐ 14.6

Formation of CC Bonds

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The crystal structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolution

The crystal structure of fructose‐1,6‐bisphosphate aldolase fromDrosophila melanogaster at 2.5A˚resolution