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Protein family
The Disulfide bond oxidoreductase D (DsbD) family is a member of the Lysine Exporter (LysE) Superfamily. A representative list of proteins belonging to
Disulfide_oxidoreductase_D
Enzyme
thioredoxin disulfide, whereas its 3 products are N,N,N-trimethylglycine, phosphate, and thioredoxin. This enzyme belongs to the family of oxidoreductases, specifically
Betaine_reductase
thioredoxin disulfide, and H2O, whereas its 3 products are glycine, phosphate, and thioredoxin. This enzyme belongs to the family of oxidoreductases, to be
Glycine_reductase
thioredoxin disulfide, and H2O, whereas its two products are L-methionine (R)-S-oxide and thioredoxin. This enzyme belongs to the family of oxidoreductases, specifically
L-methionine (R)-S-oxide reductase
L-methionine_(R)-S-oxide_reductase
Class of enzymes
reductase, protein disulfide (glutathione), protein disulfide transhydrogenase, glutathione-protein disulfide oxidoreductase, protein disulfide reductase (glutathione)
Protein-disulfide reductase (glutathione)
Protein-disulfide_reductase_(glutathione)
name glutathione amide:NAD+ oxidoreductase. This enzyme catalyses the following chemical reaction glutathione amide disulfide + NADH H+ H+ 2
Glutathione_amide_reductase
Protein family
oxidoreductin 1 (Ero1) is an oxidoreductase enzyme that catalyses the formation and isomerization of protein disulfide bonds in the endoplasmic reticulum
ER_oxidoreductin
Class of enzymes
precursor biosynthesis. This enzyme is an oxidoreductase, specifically one acting on CH or CH2 groups with a disulfide as acceptor. The systematic name of this
4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
4-hydroxy-3-methylbut-2-en-1-yl_diphosphate_synthase
Protein family
reductase EC 1.8.7.2, systematic name ferredoxin:thioredoxin disulfide oxidoreductase, is a [4Fe-4S] protein that plays an important role in the ferredoxin/thioredoxin
Ferredoxin-thioredoxin reductase
Ferredoxin-thioredoxin_reductase
Bacterial thiol disulfide oxidoreductases (TDOR) are bacterial enzymes that participate in redox reactions involving cysteine residues. Along with unfolded
List of bacterial disulfide oxidoreductases
List_of_bacterial_disulfide_oxidoreductases
Enzyme
thioredoxin disulfide, whereas its two products are 5'-adenylyl sulfate and thioredoxin. This enzyme belongs to the family of oxidoreductases, specifically
Adenylyl-sulfate reductase (thioredoxin)
Adenylyl-sulfate_reductase_(thioredoxin)
systematic name of this enzyme class is peptide-methionine:thioredoxin-disulfide S-oxidoreductase [methionine (R)-S-oxide-forming]. Other names in common use include
Peptide-methionine (R)-S-oxide reductase
Peptide-methionine_(R)-S-oxide_reductase
catalyzes the chemical reaction acetyl phosphate + methylamine + thioredoxin disulfide ⇌ {\displaystyle \rightleftharpoons } N-methylglycine + phosphate + thioredoxin
Sarcosine_reductase
Protein-coding gene in the species Homo sapiens
Protein disulfide-isomerase A3 (PDIA3), also known as glucose-regulated protein, 58-kD (GRP58), is an isomerase enzyme encoded by the autosomal gene PDIA3
PDIA3
enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with a disulfide as acceptor. The systematic
D-proline_reductase_(dithiol)
Ubiquitous antioxidant compound in living organisms
residue notation γ-ECG. It oxidizes into glutathione disulfide (GSSG), where the SS denotes the disulfide bond between two glutathiones. Glutathione biosynthesis
Glutathione
Protein-coding gene in humans
cell plasma membranes has properties of a protein disulfide-thiol oxidoreductase with protein disulfide-thiol interchange activity". Journal of Bioenergetics
Ecto-NOX disulfide-thiol exchanger 2
Ecto-NOX_disulfide-thiol_exchanger_2
disulfide reductase (FDR) superfamily. FDRs are typically characterized as being dimeric or two subunit proteins, but sulfide quinone oxidoreductase is
Sulfide:quinone_reductase
Enzyme
environment of the cell. Glutathione reductase functions as dimeric disulfide oxidoreductase and uses flavin adenine dinucleotide and nicotinamide adenine dinucleotide
Glutathione_reductase
Protein-coding gene in the species Homo sapiens
Ecto-NOX disulfide-thiol exchanger 1 is a protein that in humans is encoded by the ENOX1 gene. Electron transport pathways are generally associated with
Ecto-NOX disulfide-thiol exchanger 1
Ecto-NOX_disulfide-thiol_exchanger_1
Protein-coding gene in the species Homo sapiens
family proteins, this protein is multifunctional and acts as an oxidoreductase for disulfide formation, breakage, and isomerization. The activity of P4HB
P4HB
Trypanothione-disulfide reductase (EC 1.8.1.12) is an enzyme that catalyzes the chemical reaction trypanothione disulfide + NADPH H+ H+ trypanothione
Trypanothione-disulfide reductase
Trypanothione-disulfide_reductase
American biochemist
Williams CH Jr (2011). "Reactivity of Thioredoxin as a Protein Thiol-Disulfide Oxidoreductase". Chemical Reviews. 111 (9): 5768–5783. doi:10.1021/cr100006x.
David_Ballou
Protein-coding gene in the species Homo sapiens
D, Itin A, Gal O, Kalinski H, Feinstein E, Keshet E (February 2005). "Ero1-L alpha plays a key role in a HIF-1-mediated pathway to improve disulfide bond
ERO1L
this enzyme class is peroxiredoxin-(S-hydroxy-S-oxocysteine):thiol oxidoreductase [ATP-hydrolysing; peroxiredoxin-(S-hydroxycysteine)-forming]. Other
Sulfiredoxin
Class of reduction–oxidation proteins
glutathione rather than a specific reductase. Thioredoxin is a 12-kD oxidoreductase protein. Thioredoxin proteins also have a characteristic tertiary structure
Thioredoxin
Chemical compound
then goes on to Ecm17, an oxidoreductase, creating a disulfide bond. The last step in this biosynthesis transforms the disulfide bond into a thioacetal bridge
Echinomycin
Protein family
Zhang YY, Guan YX, Yao SJ (December 2014). "Co-expression of disulfide oxidoreductases DsbA/DsbC markedly enhanced soluble and functional expression
DsbC_protein_family
Family of bacteria
proteins bifunctional protein-disulfide isomerise/oxidoreductase DsbC, L-methionine/branched chain amino acid transporter, D-alanine-D-alanine ligase, and hypothetical
Budviciaceae
R, Ellgaard L (April 2004). "ERp57 is a multifunctional thiol-disulfide oxidoreductase". The Journal of Biological Chemistry. 279 (18): 18277–87. doi:10
Peptide-loading_complex
Metabolic enzyme PHGDH
allosteric regulation in D-3-phosphoglycerate dehydrogenase. Cross-linking adjacent regulatory domains with engineered disulfides mimics effector binding"
Phosphoglycerate dehydrogenase
Phosphoglycerate_dehydrogenase
Enzyme
acceptor. The systematic name of this enzyme class is xylitol:NADP+ 2-oxidoreductase (L-xylulose-forming). A deficiency is responsible for pentosuria. The
L-xylulose_reductase
Enzyme
acceptor. The systematic name of this enzyme class is formaldehyde:NAD+ oxidoreductase. Other names in common use include NAD+-linked formaldehyde dehydrogenase
Formaldehyde_dehydrogenase
Class of chemical compounds
further avoid confusion with disulfides with the grouping R-S-S-R, by emphasizing the presence of an H at one end of a disulfide bond. Older literature has
Persulfide
reductase EC 1.8.4.15: protein dithiol oxidoreductase (disulfide-forming) EC 1.8.4.16: thioredoxin:protein disulfide reductase EC 1.8.5.1: glutathione dehydrogenase
List_of_EC_numbers_(EC_1)
Class of enzymes
phosphate (NADPH) provides two hydrogen atoms that are used to reduce the disulfide groups of thioredoxin. Three classes of RNR have similar mechanisms for
Ribonucleotide_reductase
Protein-coding gene in the species Homo sapiens
multi-domain disulfide catalyst. Unlike other disulfide catalysts, QSOX1 can both generate disulfides de novo and catalyze dithiol/disulfide exchange. The
QSOX1
Protein-coding gene in the species Homo sapiens
multi-enzyme complexes. Additionally, DLD is a flavoenzyme oxidoreductase that contains a reactive disulfide bridge and a FAD cofactor that are directly involved
Dihydrolipoamide dehydrogenase
Dihydrolipoamide_dehydrogenase
Enzyme found in humans
oxidase is a member of the enzyme class oxidases, or more specifically, oxidoreductases. These enzymes catalyze a simultaneous oxidation-reduction reaction
Pyridoxine 5′-phosphate oxidase
Pyridoxine_5′-phosphate_oxidase
Class of enzymes
a NADPH binding domain, and an active site containing a redox-active disulfide bond. Thioredoxin reductases are enzymes that catalyze the reduction of
Thioredoxin_reductase
Protein-coding gene in humans
subsequent disulfide oxidation of SOD1. When CCS docks to SOD1, cysteine 244 of CCS and 57 of SOD1 form a disulfide linkage. This disulfide bond is then
CCS_(gene)
Class of enzymes
The systematic name of this enzyme class is AMP, sulfite:acceptor oxidoreductase (adenosine-5'-phosphosulfate-forming). Other names in common use include
Adenylyl-sulfate_reductase
Coenzyme
called oxidoreductases. The correct names for these enzymes contain the names of both their substrates: for example NADH-ubiquinone oxidoreductase catalyzes
Nicotinamide adenine dinucleotide
Nicotinamide_adenine_dinucleotide
The systematic name of this enzyme class is Mn(II):hydrogen-peroxide oxidoreductase. Other names in common use include peroxidase-M2, and Mn-dependent (NADH-oxidizing)
Manganese_peroxidase
Protein-coding gene in humans
Scoones D, Lapthorn A, Bulleid NJ, Benham AM (September 2005). "Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta"
ERO1LB
Chemical compound
s-adenosyl methionine (SAM) in the reaction GliT: oxidoreductase thioredoxin that mediates closure of the disulfide-bridge GliA: Major Facilitator Superfamily
Gliotoxin
Class of enzymes
family of isomerases, specifically a class of other intramolecular oxidoreductases. The systematic name of this enzyme class is (5,13) - (15S)-9alpha
Prostaglandin-D_synthase
Protein-coding gene in the species Homo sapiens
Kohrer K, Strack N, Mewes HW, Ottenwalder B, Obermaier B, Tampe J, Heubner D, Wambutt R, Korn B, Klein M, Poustka A (Mar 2001). "Toward a catalog of human
TXNDC2
Protein found in humans
ontology Molecular function selenium binding thioredoxin-disulfide reductase activity oxidoreductase activity Cellular component endoplasmic reticulum endoplasmic
Selenoprotein_T
Protein-coding gene in the species Homo sapiens
2016-10-26. Ye H, Jeong SY, Ghosh MC, Kovtunovych G, Silvestri L, Ortillo D, Uchida N, Tisdale J, Camaschella C, Rouault TA (2010). "Glutaredoxin 5 deficiency
GLRX5
Gene of the species Homo sapiens
Protein disulfide-isomerase TMX3 is an enzyme that in humans is encoded by the TMX3 gene. GRCm38: Ensembl release 89: ENSMUSG00000024614 – Ensembl, May
TMX3
Protein-coding gene in the species Homo sapiens
1016/j.ajhg.2012.09.018. PMC 3516600. PMID 23141294. Bunik VI, Degtyarev D (May 2008). "Structure-function relationships in the 2-oxo acid dehydrogenase
DHTKD1
Bacteria-produced protein complex and disease agent
CTA2, which remain linked by a disulfide bond between Cys187 and Cys199. The ER-resident oxidoreductase protein disulfide isomerase (PDI), with assistance
Cholera_toxin
Protein-coding gene in the species Homo sapiens
Biotechnology Information, U.S. National Library of Medicine. Lescure A, Gautheret D, Carbon P, Krol A (Feb 2000). "Novel selenoproteins identified in silico and
MSRB1
Enzyme family protecting the organism from oxidative damages
peroxidase catalyzes is: 2 glutathione H2O2 2 H2O glutathione disulfide The mechanism involves oxidation of the selenol of a selenocysteine residue
Glutathione_peroxidase
Class of enzymes
called chlorophyllide oxidoreductase (COR, (BchNB)2 + BchL2 or (BchYZ)2 + BchX2). Separately, two of the nitrogenase subunits (NifD and NifH) have homologues
Nitrogenase
Protein-coding gene in the species Homo sapiens
294 (1): E36–42. doi:10.1152/ajpendo.00352.2007. PMID 17957032. Šimčíková D, Heneberg P (December 2019). "Refinement of evolutionary medicine predictions
Pyruvate dehydrogenase (lipoamide) alpha 1
Pyruvate_dehydrogenase_(lipoamide)_alpha_1
Enzyme complex
"Mitochondrial reactive oxygen species enable proinflammatory signaling through disulfide linkage of NEMO". Science Signaling. 12 (568) eaar5926. doi:10.1126/scisignal
NADPH_oxidase
Protein-coding gene in humans
(December 2019). "COA6 Is Structurally Tuned to Function as a Thiol-Disulfide Oxidoreductase in Copper Delivery to Mitochondrial Cytochrome c Oxidase". Cell
COA6
Protein-coding gene in the species Homo sapiens
(7): 1670–1679. doi:10.1002/ijc.21572. PMID 16231315. S2CID 21916723. Guo D, Han J, Adam BL, et al. (2005). "Proteomic analysis of SUMO4 substrates in
TXNL1
Protein-coding gene in humans
Research. 63 (5): 980–986. PMID 12615712. Zhou B, Liu X, Mo X, Xue L, Darwish D, Qiu W, et al. (October 2003). "The human ribonucleotide reductase subunit
RRM2B
Class of enzymes
aspirin, a range that may be relevant for typical doses. Calcitriol (vitamin D) significantly inhibits the expression of the COX-2 gene. Caution should be
Cyclooxygenase
Protein-coding gene in humans
homodimer which forms a beta barrel (β-barrel) and contains an intramolecular disulfide bond and a binuclear Cu/Zn site in each subunit. This Cu/Zn site holds
SOD1
Class of enzymes
systematic name of this enzyme class is Oplophorus-luciferin:oxygen 2-oxidoreductase (decarboxylating). This enzyme is also called Oplophorus luciferase
Oplophorus-luciferin 2-monooxygenase
Oplophorus-luciferin_2-monooxygenase
Protein-coding gene in humans
of Medicine. "Entrez Gene: ribonucleotide reductase M2". Pavloff N, Rivard D, Masson S, Shen SH, Mes-Masson AM (1992). "Sequence analysis of the large
RRM2
Enzyme
endoplasmic reticulum. This subunit is identical to the enzyme known as protein disulfide isomerase. Prolyl hydroxylase catalyzes the formation of hydroxyproline
Procollagen-proline dioxygenase
Procollagen-proline_dioxygenase
Chemical element with atomic number 42 (Mo)
compound is molybdenum disulfide MoS2. From the perspective of commerce, the most important compounds are molybdenum disulfide (MoS 2) and molybdenum
Molybdenum
Classification of membrane proteins including ion channels
Polymerase (V-PPP) Family 5.A.1 The Disulfide Bond Oxidoreductase D (DsbD) Family 5.A.2 The Disulfide Bond Oxidoreductase B (DsbB) Family 5.A.3 The Prokaryotic
Transporter Classification Database
Transporter_Classification_Database
Class of enzymes which convert a molecule between isomeric forms
conversion of D-glucose-6-phosphate to D-fructose-6-phosphate is catalyzed by glucose-6-phosphate isomerase, an intramolecular oxidoreductase. The overall
Isomerase
(NADP) EC 1.1.1.2 Homoserine Dehydrogenase EC 1.1.1.3 Aminopropanol Oxidoreductase EC 1.1.1.4 Diacetyl Reductase EC 1.1.1.5 Glycerol Dehydrogenase EC 1
List_of_enzymes
Protein-coding gene in the species Homo sapiens
1293003. PMC 403697. PMID 12975309. Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins"
TMX1
Protein-coding gene in humans
"Entrez Gene: RRM1 ribonucleotide reductase M1 polypeptide". Pavloff N, Rivard D, Masson S, et al. (1992). "Sequence analysis of the large and small subunits
RRM1
Vesicles released from the outer membranes of Gram-negative bacteria
Host–pathogen interactions Host–pathogen interface List of bacterial disulfide oxidoreductases Virulence Toyofuku, Masanori; Nomura, Nobuhiko; Eberl, Leo (January
Outer_membrane_vesicle
Class of enzymes
GMP reductase EC 1.7.1.7 (Guanosine 5'-monophosphate oxidoreductase ) is an enzyme that catalyzes the irreversible and NADPH-dependent reductive deamination
GMP_reductase
Protein family
Peptidoglycolipid Addressing Protein (GAP) Family 5.A.1 - The Disulfide Bond Oxidoreductase D (DsbD) Family Two members of the LysE family (LysE of Corynebacterium
Lysine_exporter
Genus of bacteria
c-type cytochrome biogenesis protein CcsB, thiol-disulfide oxidoreductase ResA, hypothetical proteins, arginase, preprotein translocase subunit
Metasolibacillus
Class of enzymes
monooxygenases (EC 1.14.13), which belong to the family of monooxygenase oxidoreductases, along with the other subfamilies Baeyer-Villiger monooxygenases and
Flavin-containing monooxygenase
Flavin-containing_monooxygenase
Species of bacterium
(2019). "Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent
Chlamydia_trachomatis
Mammalian protein found in Homo sapiens
against oxidative stress. The oxidized form of glutathione (glutathione disulfide), which is generated during the reduction of hydroperoxides by GPX4, is
Glutathione_peroxidase_4
Protein-coding gene in the species Homo sapiens
Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler
GFER
Biological oxidation of ammonia/ammonium to nitrate
(hydroxylamine to nitrite) is catalyzed by two enzymes. Hydroxylamine oxidoreductase (HAO), converts hydroxylamine to nitric oxide. NH 2 OH ⟶ NO + 3 H +
Nitrification
Mammalian protein found in Homo sapiens
particular, these shared features include cysteine residues involved in disulfide bond formation, histidine residues involved in copper binding, and residues
Hephaestin
Hydrocarbon compound (C6H6)
enzymes are involved. These include cytochrome P450 2E1 (CYP2E1), quinine oxidoreductase (NQ01 or DT-diaphorase or NAD(P)H dehydrogenase (quinone 1)), GSH, and
Benzene
Class of enzymes
consumes glutathione by converting it to glutathione disulfide; the cells then metabolize glutathione disulfide back to glutathione in a glutathione reductase-dependent
5-Hydroxyeicosanoid dehydrogenase
5-Hydroxyeicosanoid_dehydrogenase
Protein-coding gene in humans
and maturation of the subunit. In addition, SCO2 acts as a thiol-disulfide oxidoreductase to regulate the redox state of the cysteines in SCO1 during maturation
SCO2
Illness from ingesting arsenic
contribute to detoxification. Arsenite inhibits members of the disulfide oxidoreductase family like glutathione reductase and thioredoxin reductase. The
Arsenic_poisoning
Post-translational modification
the free thiols in another protein. Thioredoxin (Txn), a protein disulfide oxidoreductase for the cytosol and caspase 3 are a good example where transnitrosylation
S-Nitrosylation
Human enzyme involved in inflammation
needed] COX-2 is naturally inhibited by calcitriol (the active form of vitamin D). Both the peroxidase and PTGS activities are inactivated during catalysis
Cyclooxygenase-2
Protein-coding gene in the species Homo sapiens
17-beta-dehydrogenase (NADP+) activity oxidoreductase activity androsterone dehydrogenase activity 15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity ketosteroid
AKR1C3
Chemical compound (CH3CH2CH2COOH)
is oxidized into acetyl coenzyme A catalyzed by pyruvate:ferredoxin oxidoreductase. Two molecules of carbon dioxide (CO2) and two molecules of hydrogen
Butyric_acid
Highly modified saliva containing zootoxins
(35-60%). Fraction V is structurally stable because it has seventeen disulfide bonds; it's unique in that it has the highest solubility and lowest isoelectric
Snake_venom
Membrane protein involved in transportation
membrane include two-electron carriers, such as the disulfide bond oxidoreductases (DsbB and DsbD in E. coli) as well as one-electron carriers such as
Membrane_transport_protein
Microorganisms able to reduce elemental sulfur to hydrogen sulfide
the global sulfur cycle, including methanethiol, dimethyl disulfide, and carbon disulfide. Microorganisms with sulfur-based metabolism offer a significant
Sulfur-reducing_bacteria
Mammalian protein found in humans
reductase (MTRR), which consists of flavodoxin-like and ferrodoxin-NADP+ oxidoreductase (FNR)-like domains. In many bacteria, the reduction is carried out by
Methionine_synthase
Enzyme involved in prostaglandin synthesis
PMID 1734857. Vane JR, Mitchell JA, Appleton I, Tomlinson A, Bishop-Bailey D, Croxtall J, et al. (March 1994). "Inducible isoforms of cyclooxygenase and
Cyclooxygenase-1
Class of transport proteins
glutathione-dependent oxidoreductase enzymatic activity. CLICs 1, 2 and 4 demonstrate typical glutaredoxin-like activity using 2-hydroxyethyl disulfide as a substrate
Chloride_channel
Protein family
whereas others are in prolyl 4-hydroxylases, tyrosinases, peroxidases, oxidoreductases, or proteins containing epidermal growth factor-like domains, thrombospondin-type
Stichodactyla_toxin
Protein-coding gene in humans
also referred to as 15-PGDH) is an enzyme belongs to the family of oxidoreductases, specifically the short chain dehydrogenase/reductase family 36C member
HPGD
Class of enzymes
indicates the main class that the enzyme belongs to (the options being oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases). Lysine
Lysine_carboxypeptidase
where instead of a proS gene an FAD-dependent pyridine nucleotide-disulfide oxidoreductase encoding gene was found upstream of the αr9 locus, and Mesorhizobium
Αr9_RNA
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DISULFIDE OXIDOREDUCTASE-D
DISULFIDE OXIDOREDUCTASE-D
DISULFIDE OXIDOREDUCTASE-D
DISULFIDE OXIDOREDUCTASE-D
DISULFIDE OXIDOREDUCTASE-D
DISULFIDE OXIDOREDUCTASE-D
DISULFIDE OXIDOREDUCTASE-D
DISULFIDE OXIDOREDUCTASE-D
DISULFIDE OXIDOREDUCTASE-D
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