Identification of potential redox-sensitive cysteines in cytosolic forms of fructosebisphosphatase and glyceraldehyde-3-phosphate dehydrogenase.
Tertiary-structure modeling suggests the occurrence of disulfide bonds in the cytosolic form of fructose-bisphosphatase (EC 3.1.3.11) in spinach (Spinacia oleracea L.), sugarbeet (Beta vulgaris L.) and potato (Solanum tuberosum L.). Redox modulation could then control the AMP sensitivity of fructosebisphosphatase in the cytosol, as suggested by the experiments of E. Khayat et al. (1993, Plant Physiol. 101, 57-64). Modeling also reveals two cysteine residues correctly positioned to form a disulfide bond and hence potentially redox-sensitive in the cytosolic glyceraldehyde-3-phosphate dehydrogenase (EC 1.2.1.12) from the facultative crassulacean metabolism plant Mesembryanthemum crystallinum L.
Anderson
L E
LE
Department of Biological Sciences, University of Illinois at Chicago 60607-7060, USA.
Li
D
D
Prakash
N
N
Stevens
F J
FJ
D000595:Amino Acid Sequence; D000818:Animals; D003196:Computer Graphics; D003545:Cysteine / Q000032:analysis* / Q000737:chemistry; D003600:Cytosol / Q000201:enzymology; D006597:Fructose-Bisphosphatase / Q000737:chemistry*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry*; D008969:Molecular Sequence Data; D015394:Molecular Structure; D010084:Oxidation-Reduction; D059828:Plant Cells; D010940:Plant Proteins / Q000737:chemistry*; D010944:Plants / Q000201:enzymology*; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid
D010940:Plant Proteins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases; D006597:Fructose-Bisphosphatase; D003545:Cysteine