The Enzymatic Significance of S-Acetylation and N-Acetylation of 3-Phosphoglyceraldehyde Dehydrogenase

Mathew, Elizabeth; Meriwether, Blanche P.; Park, Jane Harting

doi:10.1016/s0021-9258(18)99472-x

Cited by 59 publications

(18 citation statements)

References 34 publications

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“…Effect of Photooxidation on the 5 --N Transfer of the Acetyl Group from Cysteine to Lysine. Under the conditions of Tables I-III, namely, pH 8.0 and room temperature, acetyl phosphate acetylates the reactive cysteine-149 and then the acetyl group migrates to lysine-183 by an S N transfer reaction (Mathew et al, 1965;Mathew et al, 1967). The distribution of the acetyl groups between the cysteine and lysine moieties can be ascertained by radioautography as shown in Figure 4.…”

Section: Resultsmentioning

confidence: 99%

“…The functions of four important residues can be designated as follows: histidine-38, essential for maximum rate of deacetylation of the S-acetyl-enzyme, in the dehydrogenase, arsenolysis, and esterase activities (Bond et al, 1970;Bond and Park, 1967;Halcomb et al, 1968); cysteine-149, activesite sulfhydryl participating in the S-acetyl-enzyme formation for dehydrogenase, arsenolysis, and esterase activities (Harris et al, 1963;Mathew et al, 1967); lysine-183, acetylated in the S -N transfer reaction and involved in NAD4 binding (Mathew et al, 1965;Mathew et al, 1967); cysteine-281, essential for maintaining the proper conformation of the enzyme . Two of the critical amino acids, histidine-38 and cysteine-149, are separated by 111 residues but could readily be approximated in the folded chain.…”

Section: Resultsmentioning

confidence: 99%

“…Two of the critical amino acids, histidine-38 and cysteine-149, are separated by 111 residues but could readily be approximated in the folded chain. With the use of cross-linking reagents (Givol, 1969;Shaltiel and Tauber-Finkelstein, 1971), this has been shown to be true for the cysteine-149 and lysine-183 which are involved in the S N transfer reaction (Mathew et al, 1967;Park et al, 1970). As yet no cross-linking reagent has been found for histidine-38 and cysteine-149; however, the partial protection of the photosensitive residue by both substrate and NAD4 suggests that histidine-38 may be in the vicinity of the active center.…”

Section: Resultsmentioning

confidence: 99%

“…On the other hand, the firmly bound NAD+, which has a rigid conformation and one negative charge, must be so positioned that it does not prevent substrate interactions with the functional residues. The common property of ATP and NAD+, namely, the inhibition of the S N transfer to lysine-183, may relate to a common binding site at this residue (Mathew et al, 1967;Park et al, 1970).…”

Section: Interrelationships Between Nad+ Adenine Nucleotides and Hist...mentioning

confidence: 99%

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Effects of photooxidation of histidine-38 on the various catalytic activities of glyceraldehyde 3-phosphate dehydrogenase

Francis¹,

Meriwether²,

Park³

1973

Biochemistry

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Photooxidation of rabbit muscle glyceraIdehyde-3phosphate dehydrogenase in the presence of Rose Bengal specifically modified one histidine-38 residue per monomer and thereby inhibited the dehydrogenase, transferase, and esterase activities of this multifunctional enzyme. Glyceraldehyde-3-phosphate and NAD+ both provided partial protection against inactivation suggesting that photooxidation may occur in the vicinity of the active center. The mechanism of the inhibition has been studied by examining the catalytic steps in the various reactions. Photooxidation did not effect (1) the initial rate of oxidation of glyceraidehyde-3-phosphate to form the 5-acyl-enzyme intermediate, ( 2) the binding of the coenzyme NAD+, or (3) the S --N transfer of an acetyl group from the active-site cysteine-149 to lysine-183. Photooxidation did impair (1) the formation of the catalytically active 5-acetylenzyme intermediate with acetyl phosphate and (2) the deacetylation of the 5-acyl-enzyme complex by phosphorolysis, arsenolysis, or hydrolysis. The data indicate that the photooxidation of histidine-38 does not effect the initial oxidation step of the dehydrogenase reaction but rather the second transferase step whereby the acyl group is removed from the enzyme. The effects of photooxidation are compared to the effects of NAD+ and ATP on the active center.sing acetaldehyde as a model substrate, we have shown that the dehydrogenase reaction proceeded by a two-step mechanism (Harting and Velick, 1954a). First, the aldehyde was oxidized in the presence of the enzyme (ESH) and NAD+ to an 5-acetyl-enzyme. In the second step the acetyl group was transferred to inorganic phosphate to yield acetyl phosphate.Arsenate could substitute for phosphate to give an unstable acetyl arsenate which was hydrolyzed to acetic acid (Scheme I).In accordance with this mechanism we also demonstrated two transferase reactions which proceeded through the same acetyl-enzyme intermediate, namely, the 32P exchange and arsenolysis reactions (Harting and Velick, 1954b) (Scheme II).The enzyme is designated as ESH(NAd+) to indicate the requirements of the SH groups and NAD+ for these reactions (Harting and Velick, 1954b). The same mechanism and reactions are encountered with the biological substrate, glyceraldehyde 3-phosphate.As a further extension of these studies, the enzyme was also found to have an esterase activity in which p-nitrophenyl acetate was hydrolyzed by a two-step mechanism (Park et al., 1961) involving the formation of the common S-acetyl-enzyme Scheme I: Dehydrogenase Reaction.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Interrelationships Between Nad+ Adenine Nucleotides and Hist...mentioning

confidence: 99%

See 2 more Smart Citations

Effects of photooxidation of histidine-38 on the various catalytic activities of glyceraldehyde 3-phosphate dehydrogenase

Francis¹,

Meriwether²,

Park³

1973

Biochemistry

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show abstract

“…The reaction scheme followed in reactions catalyzed by glyceraldehyde 3-phosphate dehydrogenase involves formation of a thiol ester intermediate (Mathew et al, 1967) as in eq 2, where ES is an enzyme-substrate complex and…”

Section: Discussionmentioning

confidence: 99%