Protein disulfide isomerase, or PDI, is an enzyme in the endoplasmic reticulum (ER) in eukaryotes and the periplasm of bacteria that catalyzes the formation and breakage of disulfide bonds between cysteine residues within proteins as they fold. This allows proteins to quickly find the correct arrangement of disulfide bonds in their fully folded state, and therefore the enzyme acts to catalyze protein folding.
Thioredoxin is a class of small redox proteins known to be present in all organisms. It plays a role in many important biological processes, including redox signaling. In humans, thioredoxins are encoded by TXN and TXN2 genes. Loss-of-function mutation of either of the two human thioredoxin genes is lethal at the four-cell stage of the developing embryo. Although not entirely understood, thioredoxin is linked to medicine through their response to reactive oxygen species (ROS). In plants, thioredoxins regulate a spectrum of critical functions, ranging from photosynthesis to growth, flowering and the development and germination of seeds. Thioredoxins play a role in cell-to-cell communication.
Glutaredoxins are small redox enzymes of approximately one hundred amino-acid residues that use glutathione as a cofactor. In humans this oxidation repair enzyme is also known to participate in many cellular functions, including redox signaling and regulation of glucose metabolism. Glutaredoxins are oxidized by substrates, and reduced non-enzymatically by glutathione. In contrast to thioredoxins, which are reduced by thioredoxin reductase, no oxidoreductase exists that specifically reduces glutaredoxins. Instead, glutaredoxins are reduced by the oxidation of glutathione. Reduced glutathione is then regenerated by glutathione reductase. Together these components compose the glutathione system.
Adenylyl-sulfate reductase (thioredoxin) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-methionine (R)-S-oxide reductase (EC 1.8.4.14) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-methionine (S)-S-oxide reductase (EC 1.8.4.13) is an enzyme that catalyzes the chemical reaction
In enzymology, a peptide-methionine (R)-S-oxide reductase (EC 1.8.4.12) is an enzyme that catalyzes the chemical reaction
Protein disulfide-isomerase, also known as the beta-subunit of prolyl 4-hydroxylase (P4HB), is an enzyme that in humans encoded by the P4HB gene. The human P4HB gene is localized in chromosome 17q25. Unlike other prolyl 4-hydroxylase family proteins, this protein is multifunctional and acts as an oxidoreductase for disulfide formation, breakage, and isomerization. The activity of P4HB is tightly regulated. Both dimer dissociation and substrate binding are likely to enhance its enzymatic activity during the catalysis process.
Alcohol dehydrogenase [NADP+] also known as aldehyde reductase or aldo-keto reductase family 1 member A1 is an enzyme that in humans is encoded by the AKR1A1 gene. AKR1A1 belongs to the aldo-keto reductase (AKR) superfamily. It catalyzes the NADPH-dependent reduction of a variety of aromatic and aliphatic aldehydes to their corresponding alcohols and catalyzes the reduction of mevaldate to mevalonic acid and of glyceraldehyde to glycerol. Mutations in the AKR1A1 gene has been found associated with non-Hodgkin's lymphoma.
Glutaredoxin 2 (GLRX2) is an enzyme that in humans encoded by the GLRX2 gene. GLRX2, also known as GRX2, is a glutaredoxin family protein and a thiol-disulfide oxidoreductase that maintains cellular thiol homeostasis. This gene consists of four exons and three introns, spanned 10 kilobase pairs, and localized to chromosome 1q31.2–31.3.
Peptide methionine sulfoxide reductase (Msr) is a family of enzymes that in humans is encoded by the MSRA gene.
Methionine-R-sulfoxide reductase B2, mitochondrial is an enzyme that in humans is encoded by the MSRB2 gene. The MRSB2 enzyme catalyzes the reduction of methionine sulfoxide to methionine.
Gossypetin, also known as 3,5,7,8,3',4'-hexahydroxyflavone, is a flavonol, a type of flavonoid. It has been isolated from the flowers and the calyx of Hibiscus sabdariffa (roselle) and exhibits a strong antibacterial activity. The compound has also been found to act as an antagonist of TrkB. Recently it was shown that gossypetin has radioprotective activity.
Methionine sulfoxide is the organic compound with the formula CH3S(O)CH2CH2CH(NH2)CO2H. It is an amino acid that occurs naturally although it is formed post-translationally.
Methionine-S-oxide reductase (EC 1.8.4.5, methyl sulfoxide reductase I and II, acetylmethionine sulfoxide reductase, methionine sulfoxide reductase, L-methionine:oxidized-thioredoxin S-oxidoreductase) is an enzyme with systematic name L-methionine:thioredoxin-disulfide S-oxidoreductase. This enzyme catalyses the following chemical reaction
Dr. Herbert Weissbach NAS NAI AAM is an American biochemist/molecular biologist.
Dissimilatory sulfite reductase is an enzyme that participates in sulfur metabolism in dissimilatory sulfate reduction.
Cytochrome P450-DIT2 or CYP56A1 is one of the only three P450 enzyme found in fungi baker's yeast, the other two are CYP51F1(ERG11) and CYP61A1(ERG5) in the ergosterol biosynthesis pathway. CYP56A1 thought to catalyze the oxidation of tyrosine residues in the formation of L,L-dityrosine, a precursor of the spore wall.
Cytochrome P450, family 55, also known as CYP55, is a cytochrome P450 family in fungi supposed to derived from horizontal gene transfer of Actinomycetes CYP105 family member in the ancestor of all Dikarya. The first gene identified in this family is the CYP55A1 from Fusarium oxysporum encoding the NADPH dependent reductase of nitrous oxide.
Napin is one of the two most abundant seed storage proteins in the seeds of dicot crop mustard and rapeseed. They are water soluble low-molecular weight basic proteins classified as 2S or 1.7S proteins, representing 20–40% of total seed protein, and having a molecular weight in the range of 12–17 kDa. Their isoelectric point varies based on the method of extraction and the specific characteristics of the isoforms that exist. They are composed of two polypeptide chains, a 4.5 kDa small subunit and a large 10 kDa subunit, stabilized primarily by disulphide bonds. Their secondary structure shows a high α-helical content.
