Exploring substrate binding and discrimination in fructose1,6-bisphosphate and tagatose 1,6-bisphosphate aldolases
نویسندگان
چکیده
منابع مشابه
Structure of tagatose-1,6-bisphosphate aldolase. Insight into chiral discrimination, mechanism, and specificity of class II aldolases.
Tagatose-1,6-bisphosphate aldolase (TBPA) is a tetrameric class II aldolase that catalyzes the reversible condensation of dihydroxyacetone phosphate with glyceraldehyde 3-phosphate to produce tagatose 1,6-bisphosphate. The high resolution (1.45 A) crystal structure of the Escherichia coli enzyme, encoded by the agaY gene, complexed with phosphoglycolohydroxamate (PGH) has been determined. Two s...
متن کاملStructure of Class II Tagatose - 1 , 6 - bisphosphate Aldolase 22019
ion of a proton from DHAP C1 would be feasible. Glu of FBPA corresponds to Glu in TBPA, which is also positioned on a glycine-rich loop. Due to the lack of reliable electron density, this residue has not been included in the TBPA model and it is presumed to be flexible and disordered. The sequence conservation of this loop in TBPA and FBPA is high (Fig. 2), which implies that Glu could adopt a ...
متن کاملThe fructose-1,6-bisphosphate aldolases: same reaction, different enzymes.
Two forms of the enzyme fructoseI ,6-bisphosphate aldolase (EC 4. I .2.13) are known, designated class I and class 11. The enzymes o f class I function by imine formation between the substrate and a catalytically essential lysine residue in the active site, which acts to stabilize the intermediate carbanion (for review, see [ I , 21). The enzymes of class I1 utilize a divalent metal ion to act ...
متن کاملCrystal structure of activated ribulose-1,5-bisphosphate carboxylase complexed with its substrate, ribulose-1,5-bisphosphate.
The three-dimensional structure of the complex of ribulose-1,5-bisphosphate carboxylase from Rhodospirillum rubrum, CO2, Mg2+, and ribulose bisphosphate has been determined with x-ray crystallographic methods to 2.6-A resolution. Ribulose-1,5-bisphosphate binds across the active site with the two phosphate groups in the two phosphate binding sites of the beta/alpha barrel. The oxygen atoms of t...
متن کاملStructural insights into the substrate binding and stereoselectivity of giardia fructose-1,6-bisphosphate aldolase.
Giardia lamblia fructose-1,6-bisphosphate aldolase (FBPA) is a member of the class II zinc-dependent aldolase family that catalyzes the cleavage of d-fructose 1,6-bisphosphate (FBP) into dihydroxyacetone phosphate (DHAP) and d-glyceraldehyde 3-phosphate (G3P). In addition to the active site zinc, the catalytic apparatus of FBPA employs an aspartic acid, Asp83 in the G. lamblia enzyme, which whe...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 2000
ISSN: 0014-2956
DOI: 10.1046/j.1432-1327.2000.01191.x