AFMID
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Official Full Name
arylformamidase
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Synonyms
AFMID;arylformamidase;20910;ENSG00000183077;KF;17q25.3;MGC167063, DKFZp686F03259;probable arylformamidase;probable arylformamidase;kynurenine formamidase;EC 3.5.1.9;
- Recombinant Proteins
- Cell & Tissue Lysates
- Protein Pre-coupled Magnetic Beads
- Human
- Mouse
- Zebrafish
- E.coli
- HEK293
- HEK293T
- In Vitro Cell Free System
- Mammalian Cell
- Mammalian cells
- Wheat Germ
- Flag
- GST
- His
- His (Fc)
- Avi
- Myc
- DDK
- Myc|DDK
- N/A
- N
- Involved Pathway
- Protein Function
- Interacting Protein
AFMID involved in several pathways and played different roles in them. We selected most pathways AFMID participated on our site, such as Glyoxylate and dicarboxylate metabolism, Histidine, lysine, phenylalanine, tyrosine, proline and tryptophan catabolism, L-kynurenine degradation, which may be useful for your reference. Also, other proteins which involved in the same pathway with AFMID were listed below. Creative BioMart supplied nearly all the proteins listed, you can search them on our site.
Pathway Name | Pathway Related Protein |
---|---|
Glyoxylate and dicarboxylate metabolism | GCSH;ACAT1;MUT;GRHPR;ACO1;PCCA;CAT;GCSHA;HOGA1 |
Histidine, lysine, phenylalanine, tyrosine, proline and tryptophan catabolism | PCBD1;SLC25A21;AMDHD1;UROC1;CRYM;DLST;FTCD;IDO2;AFMID |
L-kynurenine degradation | AFMID;IDO2;ACMSD |
Metabolic pathways | IDH3G;MAN1C1;ASAH1A;CYP3A41B;DCT;GSTZ1;PIGF;SDHD;ACAA1A |
Metabolism | UGT1B5;ISCUB;CTRB1;BSG;FIG4;PROZA;PDK2B;CTRC;MED31 |
Metabolism of amino acids and derivatives | FTCD;ACMSD;AFMID;AMDHD1;SLC25A15;NAGS;SLC25A15A;CKB;IVD |
NAD de novo biosynthesis | IDO2;AFMID |
Tryptophan catabolism | AFMID;IDO2 |
AFMID has several biochemical functions, for example, arylformamidase activity. Some of the functions are cooperated with other proteins, some of the functions could acted by AFMID itself. We selected most functions AFMID had, and list some proteins which have the same functions with AFMID. You can find most of the proteins on our site.
Function | Related Protein |
---|---|
arylformamidase activity |
AFMID 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 AFMID here. Most of them are supplied by our site. Hope this information will be useful for your research of AFMID.
- Q&As
- Reviews
Q&As (20)
Ask a questionDysregulation or dysfunction of AFMID protein is implicated in human diseases, and associations can be investigated using disease models, patient samples, or genetically modified systems, combined with phenotypic assessments or molecular analysis techniques.
The enzymatic activity of AFMID protein can be measured or characterized using biochemical assays or enzymatic activity assays specific to its function.
AMDHD1 possesses enzymatic activity, such as hydrolase or esterase activity, and exhibits specificity towards specific lipid substrates.
AFMID protein can be targeted or modulated to manipulate specific metabolic pathways or alleviate disease conditions, and its therapeutic potential can be evaluated using in vitro or in vivo models, combined with functional assays or disease outcome measures.
Modulating AMDHD1 activity or expression may hold therapeutic potential for metabolic disorders, providing opportunities for developing interventions that target lipid metabolism or oxidative stress-related pathways.
AFMID protein influences downstream metabolic pathways or cellular processes, which can be investigated through metabolomic profiling, genetic or pharmacological perturbations, or functional assays specific to the pathways of interest.
AMDHD1 interacts with other proteins involved in lipid metabolism, such as enzymes or transporters, and these interactions modulate cellular processes such as lipid synthesis, degradation, or transport.
AMDHD1 expression is regulated at transcriptional and post-transcriptional levels, influenced by hormonal signals, nutritional status, or cellular stresses.
AMDHD1 exhibits a tissue-specific expression pattern, with higher levels observed in tissues with active lipid metabolism, suggesting its involvement in lipid-related processes.
The enzymatic function and protein interactions of AMDHD1 are dependent on its unique structural features, including catalytic residues and protein interaction domains.
AFMID protein participates in cellular redox balance or oxidative stress response, and its involvement in these processes can be investigated using techniques such as redox assays, ROS detection, or genetic manipulations combined with functional assessments.
AMDHD1 plays a role in lipid metabolism by participating in the breakdown or remodeling of specific lipid molecules, contributing to lipid homeostasis.
The structural features or domains of AFMID protein contribute to its enzymatic activity or substrate specificity, and their functional roles can be investigated using techniques such as protein structure determination, site-directed mutagenesis, or biochemical assays.
The expression of AFMID protein is regulated by specific factors and signaling pathways that control its transcriptional or post-transcriptional regulation.
AMDHD1 deficiency or dysregulation may lead to altered lipid metabolism, mitochondrial dysfunction, or cellular stress, potentially contributing to metabolic disorders or other related diseases.
Genetic variations or mutations in the gene encoding AFMID protein may impact its expression or function, leading to altered susceptibility to diseases or metabolic disorders, and these can be studied through genetic association studies or functional characterization of mutant variants.
AFMID protein interacts with endogenous substrates or metabolites, and their interactions can be studied or quantified using techniques such as mass spectrometry, metabolomics analysis, or enzymatic assays.
AMDHD1 contributes to maintaining cellular redox balance by participating in lipid metabolism pathways linked to antioxidant defense mechanisms.
AMDHD1 activity can influence downstream signaling pathways, including those involved in lipid signaling, cellular energy homeostasis, or inflammation.
Post-translational modifications or regulatory mechanisms may modulate the activity or stability of AFMID protein, and these can be studied using techniques such as site-directed mutagenesis, phosphoproteomics analysis, or biochemical assays.
Customer Reviews (3)
Write a reviewUnraveling protein-protein interactions in lipid metabolism for metabolic disorders.
Elucidating protein-protein interactions in cell adhesion for tissue morphogenesis.
Exploring protein-protein interactions in neurodegenerative diseases for therapeutic targets.
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