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Literature summary for 5.3.4.1 extracted from

  • Hernandez, G.; Anderson, J.S.; LeMaster, D.M.
    Electrostatic stabilization and general base catalysis in the active site of the human protein disulfide isomerase a domain monitored by hydrogen exchange (2008), ChemBioChem, 9, 768-778.
    View publication on PubMed
Search for more literature for 5.3.4.1

Cloned(Commentary)

Cloned (Comment) Organism
expression of protein disulfide isomerase a domain in Escherichia coli Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
molecular modeling offers a role for the conserved residue R103 in coordinating the oxidative transition-state complex Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P07237
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Reaction

Reaction Comment Organism Reaction ID
catalyses the rearrangement of -S-S- bonds in proteins the nucleophilic C36 thiol of the protein disulfide isomerase a domain is positioned over the N-terminus of the alpha2 helix. The H38 amide in the reduced enzyme exhibits a maximum rate of exchange at pH 5 due to efficient general base catalysis by the neutral imidazole of its own side chain and suppression of its exchange by the ionization of the C36 thiol. Ionization of this thiol and deprotonation of the H38 side chain suppress the C39 amide hydroxide-catalyzed exchange by a million-fold. The electrostatic potential within the active site stabilizes the two distinct transition states that lead to substrate reduction and oxidation Homo sapiens
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the nucleophilic C36 thiol of the protein disulfide isomerase a domain is positioned over the N-terminus of the alpha2 helix. The H38 amide in the reduced enzyme exhibits a maximum rate of exchange at pH 5 due to efficient general base catalysis by the neutral imidazole of its own side chain and suppression of its exchange by the ionization of the C36 thiol. Ionization of this thiol and deprotonation of the H38 side chain suppress the C39 amide hydroxide-catalyzed exchange by a million-fold. The electrostatic potential within the active site stabilizes the two distinct transition states that lead to substrate reduction and oxidation Homo sapiens ?
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