Mechanism of allosteric activation of glycogen phosphorylase probed by the reactivity of essential arginine residues. Identification of an arginine residue involved in the binding of glucose 1-phosphate

Vandenbunder, Bernard; Dreyfus, Marc; Bertrand, Olivier; Dognin, May J.; Sibilli, Lise; Buc, Henri

doi:10.1021/bi00511a044

Cited by 14 publications

(11 citation statements)

References 33 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The latter two amino acids may react with phenylglyoxal under some conditions (Takahashi, 1968(Takahashi, , 1977a). The partial regeneration of arginine during acid hydrolysis has been reported (Vandenbunder et al, 1981). The sulfhydryl content determined with 5,5'-dithiobis(2-nitrobenzoic acid) in the presence of 0.1% sodium dodecyl sulfate (Ellman, 1959) is unchanged by modification (data not shown).…”

Section: Competition Between Phenylglyoxal and L-serine Formentioning

confidence: 76%

See 1 more Smart Citation

L-Serine binds to arginine-148 of the .beta.2 subunit of Escherichia coli tryptophan synthase

Tanizawa¹,

Miles²

1983

Biochemistry

View full text Add to dashboard Cite

Inactivation of the beta 2 subunit and of the alpha 2 beta 2 complex of tryptophan synthase of Escherichia coli by the arginine-specific dicarbonyl reagent phenylglyoxal results from modification of one arginyl residue per beta monomer. The substrate L-serine protects the holo beta 2 subunit and the holo alpha 2 beta 2 complex from both inactivation and arginine modification but has no effect on the inactivation or modification of the apo forms of the enzyme. This result and the finding that phenylglyoxal competes with L-serine in reactions catalyzed by both the holo beta 2 subunit and the holo alpha 2 beta 2 complex indicate that L-serine and phenylglyoxal both bind to the same essential arginyl residue in the holo beta 2 subunit. The apo beta 2 subunit is protected from phenylglyoxal inactivation much more effectively by phosphopyridoxyl-L-serine than by either pyridoxal phosphate or pyridoxine phosphate, both of which lack the L-serine moiety. The phenylglyoxal-modified apo beta 2 subunit binds pyridoxal phosphate and the alpha subunit but cannot bind L-serine or L-tryptophan. We conclude that the alpha-carboxyl group of L-serine and not the phosphate of pyridoxal phosphate binds to the essential arginyl residue in the beta 2 subunit. The specific arginyl residue in the beta 2 subunit which is protected by L-serine from modification by phenyl[2-14C]glyoxal has been identified as arginine-148 by isolating a labeled cyanogen bromide fragment (residues 135-149) and by digesting this fragment with pepsin to yield the labeled dipeptide arginine-methionine (residues 148-149). The primary sequence near arginine-148 contains three other basic residues (lysine-137, arginine-141, and arginine-150) which may facilitate anion binding and increase the reactivity of arginine-148. The conservation of the arginine residues 141, 148, and 150 in the sequences of tryptophan synthase from E. coli, Salmonella typhimurium, and yeast supports a functional role for these three residues in anion binding. The location and role of the active-site arginyl residues in the beta 2 subunit and in two other enzymes which contain pyridoxal phosphate, aspartate aminotransferase and glycogen phosphorylase, are compared.

show abstract

Section: Competition Between Phenylglyoxal and L-serine Formentioning

confidence: 76%

“…The functional arginyl residue has been located in the sequence of only two enzymes which contain pyridoxal phosphate: glycogen phosphorylase (Vandenbunder et al, 1981) and aspartate aminotransferase (Sandmeier & Christen, 1982).…”

mentioning

confidence: 99%

L-Serine binds to arginine-148 of the .beta.2 subunit of Escherichia coli tryptophan synthase

Tanizawa¹,

Miles²

1983

Biochemistry

View full text Add to dashboard Cite

show abstract

“…13 (Riordan, 1979) . In some studies, however, a 1 :1 stoichiometry has been reported (Borders and Riordan, 1975 ;Werber et al, 1975 ;Kazarinoff and Snell, 1976 ;Philips et al, 1979 ;Vandenbunder et al, 1981) . These 1 :1 stoichiometries have usually been found under conditions of low phenylglyoxal concentration (Borders and Riordan, 1975) or in the presence of borate buffer (Werber et al, 1975 ;Kazarinoff and Snell, 1976 ;Vandenbunder et al, 1981) .…”

Section: Reaction Ofarginyl Residues With Phenylglyoxalmentioning

confidence: 97%

“…In some studies, however, a 1 :1 stoichiometry has been reported (Borders and Riordan, 1975 ;Werber et al, 1975 ;Kazarinoff and Snell, 1976 ;Philips et al, 1979 ;Vandenbunder et al, 1981) . These 1 :1 stoichiometries have usually been found under conditions of low phenylglyoxal concentration (Borders and Riordan, 1975) or in the presence of borate buffer (Werber et al, 1975 ;Kazarinoff and Snell, 1976 ;Vandenbunder et al, 1981) . Borate can presumably complex the cis-diol of Selective Modification ofthe Anion Transport System Scheme for the reaction of the guanidine free-base of an arginyl residue with phenylglyoxal.…”

Section: Reaction Ofarginyl Residues With Phenylglyoxalmentioning

confidence: 99%

“…6 and 9) . This selectivity can be compared to the remarkable selectivity of phenylglyoxal for modification of only the functionally essential arginyl residues at enzyme active sites, as many enzymes can be fully inactivated by phenylglyoxal after modification of a single arginyl residue per enzyme protomer or subunit (Borders and Riordan, 1975 ;Berghauser, 1975 ;Armstrong et al, 1976 ;Kantrowitz and Lipscomb, 1976 ;Philips et al, 1979;Cheung and Fonda, 19796;Borders and Johansen, 1980a, b ;Vandenbunder et al, 1981) . Phenylglyoxal is not an "affinity" reagent or an "active-site-directed" reagent, for most studies using this reagent show that rates of inactivation of enzymes are first order in phenylglyoxal.…”

Section: Stoichiometry Between Phenylglyoxal Binding and Transport Inactivationmentioning

confidence: 99%

See 1 more Smart Citation

Selective phenylglyoxalation of functionally essential arginyl residues in the erythrocyte anion transport protein.

Bjerrum¹,

Wieth²,

Borders³

1983

The Journal of General Physiology

View full text Add to dashboard Cite

The red cell anion transport protein, band 3, can be selectively modified with phenylglyoxal, which modifies arginyl residues (arg) in proteins, usually with a phenylglyoxal :arg stoichiometry of 2 :1 . Indiscriminate modification of all arg in red cell membrane proteins occurred rapidly when both extra-and intracellular pH were above 10 . Selective modification of extracellularly exposed arg was achieved when ghosts with a neutral or acid intracellular pH were treated with phenylglyoxal in an alkaline medium . The rate and specificity of modification depend on the extracellular chloride concentration . At 165 mM chloride maximum transport inactivation was accompanied by the binding of four phenylglyoxals per band 3 molecule. After removal of extracellular chloride, maximum transport inhibition was accompanied by the incorporation of two phenylglyoxals per band 3, which suggests that transport function is inactivated by the modification of a single arg . After cleavage of band 3 with extracellular chymotrypsin, [14 C]phenylglyoxal was located almost exclusively in a 35,000-dalton peptide . In contrast, the primary covalent binding site of the isothiocyanostilbenedisulfonates is a lysyl residue in the second cleavage product, a 65,000-dalton fragment. This finding supports the view that the transport region of band 3 is composed of strands from both chymotryptic fragments . The binding of phenylglyoxal and the stilbene inhibitors interfered with each other. The rate of phenylglyoxal binding was reduced by a reversibly binding stilbenedisulfonate (DNDS), and covalent binding of [3 H]DIDS to phenylglyoxal-modified membranes was strongly delayed . At DIDS concentrations below 10 j,M, only 50% of the band 3 molecules were labeled with [ 3H]-DIDS during 90 min at 38°C, thereby demonstrating an interaction between binding of the two inhibitors to the protomers of the oligomeric band 3 molecules .

show abstract

Higher Plant Phosphorylases

Tanizawa

Mori

Tagaya

et al. 1994

Molecular Aspects of Enzyme Catalysis

View full text Add to dashboard Cite

Mechanism of allosteric activation of glycogen phosphorylase probed by the reactivity of essential arginine residues. Identification of an arginine residue involved in the binding of glucose 1-phosphate

Cited by 14 publications

References 33 publications

L-Serine binds to arginine-148 of the .beta.2 subunit of Escherichia coli tryptophan synthase

L-Serine binds to arginine-148 of the .beta.2 subunit of Escherichia coli tryptophan synthase

Selective phenylglyoxalation of functionally essential arginyl residues in the erythrocyte anion transport protein.

Higher Plant Phosphorylases

Contact Info

Product

Resources

About