ADH5
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Official Full Name
alcohol dehydrogenase 5 (class III), chi polypeptide
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Overview
This gene encodes a member of the alcohol dehydrogenase family. Members of this family metabolize a wide variety of substrates, including ethanol, retinol, other aliphatic alcohols, hydroxysteroids, and lipid peroxidation products. The encoded protein forms a homodimer. It has virtually no activity for ethanol oxidation, but exhibits high activity for oxidation of long-chain primary alcohols and for oxidation of S-hydroxymethyl-glutathione, a spontaneous adduct between formaldehyde and glutathione. This enzyme is an important component of cellular metabolism for the elimination of formaldehyde, a potent irritant and sensitizing agent that causes lacrymation, rhinitis, pharyngitis, and contact dermatitis. The human genome contains several non-transcribed pseudogenes related to this gene. -
Synonyms
ADH5; alcohol dehydrogenase 5 (class III), chi polypeptide; FDH, formaldehyde dehydrogenase; alcohol dehydrogenase class-3; ADH 3; ADHX; Alcohol dehydrogenase (class III) chi polypeptide; alcohol dehydrogenase 5 (class III) chi polypeptide; Alcohol dehydrogenase class 3; Alcohol dehydrogenase class chi chain; Alcohol dehydrogenase class III; class III alcohol dehydrogenase 5 chi subunit; FDH; formaldehyde dehydrogenase; Glutathione dependent formaldehyde dehydrogenase; hydroxymethyllutathione dehydrogenase; OTTHUMP00000219913; alcohol dehydrogenase class-III; S-(hydroxymethyl)glutathione dehydrogenase; glutathione-dependent formaldehyde dehydrogenase; alcohol dehydroge; ADH-3; FALDH; GSNOR; GSH-FDH;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Chicken
- Human
- Mouse
- Rat
- Zebrafish
- E. coli
- E.coli
- E.Coli or Yeast
- HEK293
- HEK293T
- In Vitro Cell Free System
- Mammalian Cell
- Mammalian cells
- Wheat Germ
- Yeast
- Flag
- GST
- His
- His (Fc)
- Avi
- Myc
- DDK
- MYC
- Myc|DDK
- N/A
- No tag
- Involved Pathway
- Protein Function
- Interacting Protein
ADH5 involved in several pathways and played different roles in them. We selected most pathways ADH5 participated on our site, such as Biological oxidations, Biosynthesis of antibiotics, Carbon metabolism, which may be useful for your reference. Also, other proteins which involved in the same pathway with ADH5 were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
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Biological oxidations | CYP3A5;Sult2a2;CYP3A7;ADH8A;CYP7A1;CYP2N13;AKR1A1;CYP4T8;GLYAT |
Biosynthesis of antibiotics | UAP1L1;AK8;BPNT1;GALM;LDHAL6B;AK7;ANI_1_2390104;EHHADH;SDSL |
Carbon metabolism | IDH2;TKTB;PFKMB;MCEE;GOT2;HAO1;RPE;FH;FBP1 |
Chemical carcinogenesis | ADH1;CYP2C39;CYP2C37;MGST2;ADH5;GSTP1;UGT1A7C;CYP3A7-CYP3AP1;GSTO2 |
Degradation of aromatic compounds | AKR1A1A;AKR1A1;RGN;ADH5;AKR1A1B |
Drug metabolism - cytochrome P450 | ADH1C;ADH5;CYP2E1;GSTK1;CYP3A5;GSTO2;ADH4;CYP2C8;ADH2-1 |
Ethanol oxidation | ADH1B;ADH1C;ADH1A;ADH4;ADH8A;ADH6;ADH5;ADH8B;ADH7 |
Fatty acid degradation | ADH1A;ADH1;ADH7;ADH4;ACSL4B;GCDHA;PECI;ACOX1;ALDH3A2A |
ADH5 has several biochemical functions, for example, S-(hydroxymethyl)glutathione dehydrogenase activity, alcohol dehydrogenase (NAD) activity, electron carrier activity. Some of the functions are cooperated with other proteins, some of the functions could acted by ADH5 itself. We selected most functions ADH5 had, and list some proteins which have the same functions with ADH5. You can find most of the proteins on our site.
Function | Related Protein |
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S-(hydroxymethyl)glutathione dehydrogenase activity | |
alcohol dehydrogenase (NAD) activity | ADH6;ADH1A;ADH7;ADH8A;ADH1C;ADH8B;ADH1;ADH5;DHRS9 |
electron carrier activity | AOC2;DHDH;NCF2;XDH;GLDC;AKR1A1;AKR7A3;GPX2;FDX1B |
fatty acid binding | FABP1;FABP2;FABP10A;FABP5;NDUFAB1;PTGDS;FABP4;ADH5;HNF4A |
formaldehyde dehydrogenase activity | ADH5;ADH8B |
protein homodimerization activity | RBM44;PON3;FGFR1OP;NOS1;ERCC5;FLNA;SRM;BMP4;NRF1 |
zinc ion binding | S100A5;S100A12;RC3H1;FBXO11A;RNF183;TRIM31;ADAM1B;TRIM63;NANOS2 |
ADH5 has direct interactions with proteins and molecules. Those interactions were detected by several methods such as yeast two hybrid, co-IP, pull-down and so on. We selected proteins and molecules interacted with ADH5 here. Most of them are supplied by our site. Hope this information will be useful for your research of ADH5.
VTN; ESRRA; ARNT; CSNK2B; PRDX1; CHD3; PQLC1; HDAC1
- Q&As
- Reviews
Q&As (10)
Ask a questionADH5 exhibits a tissue-specific expression pattern, and its expression is regulated by various factors such as transcriptional control and signaling pathways.
ADH5 can efficiently metabolize different alcohol substrates, and its substrate specificity may differ from other ADH enzymes.
ADH5 expression and activity can be influenced by chronic alcohol exposure or withdrawal, and studying the underlying molecular mechanisms can shed light on alcohol-related effects.
The activity or function of ADH5 can potentially be modulated by pharmacological agents or environmental factors, presenting potential therapeutic implications.
Interacting proteins or cofactors can modulate the activity or function of ADH5, and investigating the molecular mechanisms involved can enhance our understanding of its regulation.
The enzymatic kinetics and catalytic properties of ADH5 contribute to its overall activity and efficiency in alcohol metabolism.
ADH5 may have implications in the metabolism of other endogenous compounds or xenobiotics, suggesting its involvement in broader physiological functions.
Genetic variations or polymorphisms in the ADH5 gene may impact alcohol metabolism and susceptibility to alcohol-related disorders, emphasizing the role of genetic factors in its function.
The structural features of ADH5 play a crucial role in its catalytic activity and binding affinity for alcohol, and understanding these features provides insights into its function.
Exploring the consequences of ADH5 deficiency or overexpression provides insights into its role in alcohol metabolism and its impact on physiological processes.
Customer Reviews (2)
Write a reviewHighly effective in stabilizing and enhancing the activity of enzymes in enzyme engineering.
Demonstrates excellent resistance to aggregation and aggregation-prone conditions.
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