scholarly journals Tyrosine substitution of a conserved active-site histidine residue activates Plasmodium falciparum peroxiredoxin 6

2018 ◽  
Vol 28 (1) ◽  
pp. 100-110
Author(s):  
Kristina Feld ◽  
Fabian Geissel ◽  
Linda Liedgens ◽  
Robin Schumann ◽  
Sandra Specht ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Active Site ◽  
Histidine Residue ◽  
Peroxiredoxin 6 ◽  
Active Site Histidine

scholarly journals The location of the active-site histidine residue in the primary sequence of papain

1968 ◽  
Vol 108 (5) ◽  
pp. 861-866 ◽  
Author(s):  
S. S. Husain ◽  
G. Lowe
Keyword(s):  
Amino Acid ◽  
Sodium Borohydride ◽  
Active Site ◽  
Iodoacetic Acid ◽  
Cysteine Residue ◽  
Histidine Residue ◽  
Primary Sequence ◽  
Active Site Cysteine ◽  
Active Site Histidine ◽  
Active Site Cysteine Residue

Papain that had been irreversibly inhibited with 1,3-dibromo[2−14C]acetone was reduced with sodium borohydride and carboxymethylated with iodoacetic acid. After digestion with trypsin and α-chymotrypsin the radioactive peptides were purified chromatographically. Their amino acid composition indicated that cysteine-25 and histidine-106 were cross-linked. Since cysteine-25 is known to be the active-site cysteine residue, histidine-106 must be the active-site histidine residue.

Structural basis for the binding of succinate to succinyl-CoA synthetase

2016 ◽  
Vol 72 (8) ◽  
pp. 912-921 ◽  
Author(s):  
Ji Huang ◽  
Marie E. Fraser
Keyword(s):  
Citric Acid ◽  
Binding Site ◽  
Active Site ◽  
Citric Acid Cycle ◽  
Histidine Residue ◽  
Acid Cycle ◽  
Carboxy Terminal Domain ◽  
Carboxy Terminal ◽  
Active Site Histidine ◽  
Succinyl Coa Synthetase

Succinyl-CoA synthetase catalyzes the only step in the citric acid cycle that provides substrate-level phosphorylation. Although the binding sites for the substrates CoA, phosphate, and the nucleotides ADP and ATP or GDP and GTP have been identified, the binding site for succinate has not. To determine this binding site, pig GTP-specific succinyl-CoA synthetase was crystallized in the presence of succinate, magnesium ions and CoA, and the structure of the complex was determined by X-ray crystallography to 2.2 Å resolution. Succinate binds in the carboxy-terminal domain of the β-subunit. The succinate-binding site is near both the active-site histidine residue that is phosphorylated in the reaction and the free thiol of CoA. The carboxy-terminal domain rearranges when succinate binds, burying this active site. However, succinate is not in position for transfer of the phosphoryl group from phosphohistidine. Here, it is proposed that when the active-site histidine residue has been phosphorylated by GTP, the phosphohistidine displaces phosphate and triggers the movement of the carboxylate of succinate into position to be phosphorylated. The structure shows why succinyl-CoA synthetase is specific for succinate and does not react appreciably with citrate nor with the other C4-dicarboxylic acids of the citric acid cycle, fumarate and oxaloacetate, but shows some activity with L-malate.

scholarly journals Inactivation of prolyl endopeptidase by a peptidylchloromethane. Kinetics of inactivation and identification of sites of modification

1991 ◽  
Vol 276 (3) ◽  
pp. 837-840 ◽  
Author(s):  
S R Stone ◽  
D Rennex ◽  
P Wikstrom ◽  
E Shaw ◽  
J Hofsteenge
Keyword(s):  
Active Site ◽  
Kinetic Mechanism ◽  
Cysteine Residue ◽  
Prolyl Endopeptidase ◽  
Histidine Residue ◽  
Progress Curve ◽  
Kinetics Of ◽  
Active Site Histidine

The kinetics of inactivation of prolyl endopeptidase by acetyl-Ala-Ala-Pro-CH2Cl were studied by progress-curve methods in the presence of substrate. The kinetic mechanism was found to involve the formation of an initial complex between the enzyme and the chloromethane followed by an inactivation step. The substrate was shown to compete for the formation of the initial complex, indicating that binding at the active site was a prerequisite for inactivation. After reaction of the enzyme with [3H]acetyl-Ala-Ala-Pro-CH2Cl, it was possible to isolate five labelled peptides. Four of these peptides contained a cysteine residue as the site of modification, whereas the fifth peptide contained no cysteine and a histidine residue was identified as the site of modification. This residue (His-680) probably represents the active-site histidine of prolyl endopeptidase.

Two Glutamate Residues, Glu 208α and Glu 197β, Are Crucial for Phosphorylation and Dephosphorylation of the Active-Site Histidine Residue in Succinyl-CoA Synthetase†

Biochemistry ◽  
2002 ◽  
Vol 41 (2) ◽  
pp. 537-546 ◽  
Author(s):  
Marie E. Fraser ◽  
Michael A. Joyce ◽  
David G. Ryan ◽  
William T. Wolodko
Keyword(s):  
Active Site ◽  
Histidine Residue ◽  
Active Site Histidine ◽  
Succinyl Coa Synthetase

scholarly journals Acetyl-coenzyme A:alpha-glucosaminide N-acetyltransferase. Evidence for an active site histidine residue.

1986 ◽  
Vol 261 (22) ◽  
pp. 10127-10132
Author(s):  
K J Bame ◽  
L H Rome
Keyword(s):  
Active Site ◽  
Histidine Residue ◽  
Acetyl Coenzyme ◽  
Active Site Histidine

scholarly journals Malate dehydrogenase of the cytosol. Ionizations of the enzyme-reduced-coenzyme complex and a comparison with lactate dehydrogenase

1978 ◽  
Vol 173 (2) ◽  
pp. 597-605 ◽  
Author(s):  
A Lodola ◽  
D M Parker ◽  
R Jeck ◽  
J J Holbrook
Keyword(s):  
Lactate Dehydrogenase ◽  
Malate Dehydrogenase ◽  
Active Site ◽  
Histidine Residue ◽  
Histidine Residues ◽  
Coenzyme Binding ◽  
Active Site Histidine

1. The pH-dependencies of the binding of NADH and reduced nicotinamide–benzimidazole dinucleotide to pig heart cytoplasmic malate dehydrogenase and lactate dehydrogenase are reported. 2. Two ionizing groups were observed in the binding of both reduced coenzymes to lactate dehydrogenase. One group, with pKa in the range 6.3–6.7, is the active-site histidine residue and its deprotonation weakens binding of reduced coenzyme 3-fold. Binding of both coenzymes is decreased to zero when a second group, of pKa 8.9, deprotonates. This group is not cysteine-165.3. Only one ionization is required to characterize the binding of the two reduced coenzymes to malate dehydrogenase. The group involved appears to be the active-site histidine residue, since its ethoxycarbonylation inhibits the enzyme and abolishes binding of reduced coenzyme. Binding of either reduced coenzyme increases the pKa of the group from 6.4 to 7.4, and deprotonation of the group is accompanied by a 10-fold weakening of coenzyme binding. 4. Two reactive histidine residues were detected per malate dehydrogenase dimer. 5. A mechanism which emphasizes the homology between the two enzymes is presented.

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