Acyl Carrier Protein
Protein S
Pantetheine
Fatty Acid Synthase, Type II
3-Oxoacyl-(Acyl-Carrier-Protein) Synthase
Polyketide Synthases
Acyl-Carrier Protein S-Malonyltransferase
Acyltransferases
Acetyltransferases
Fatty Acid Synthases
Transferases (Other Substituted Phosphate Groups)
3-Oxoacyl-(Acyl-Carrier-Protein) Reductase
Escherichia coli
Molecular Sequence Data
Pantothenic Acid
Carrier Proteins
Protein S Deficiency
Amino Acid Sequence
Enoyl-(Acyl-Carrier-Protein) Reductase (NADH)
Carbon-Sulfur Ligases
Ribosomal Protein S6
Fatty Acids
Malonyl Coenzyme A
Triclosan
Base Sequence
Histone Acetyltransferases
Choline O-Acetyltransferase
Cloning, Molecular
Sequence Homology, Amino Acid
Substrate Specificity
Streptomyces
Acetyl Coenzyme A
Ribosomal Proteins
Cerulenin
Saccharopolyspora
Models, Molecular
Acyl Coenzyme A
Apoproteins
Chloramphenicol O-Acetyltransferase
Multienzyme Complexes
Anthraquinones
Acyl-Carrier Protein S-Acetyltransferase
Coriandrum
Protein Conformation
Thioctic Acid
Binding Sites
Protein Structure, Tertiary
Mutation
Crystallography, X-Ray
Protein Binding
Lipid A
Naphthacenes
p300-CBP Transcription Factors
Peptide Synthases
Plants
Carnitine O-Acetyltransferase
Electrophoresis, Polyacrylamide Gel
Sequence Alignment
Genetic Complementation Test
Ligases
Plasmids
Multigene Family
Protein C
Vibrio
Carrier State
Serine O-Acetyltransferase
Nuclear Magnetic Resonance, Biomolecular
Biocatalysis
Protein Structure, Secondary
N-Terminal Acetyltransferase A
Magnetic Resonance Spectroscopy
Macrolides
N-Terminal Acetyltransferase E
DNA Primers
Complement Inactivator Proteins
Polyketides
Molecular Structure
Alcohol Oxidoreductases
Glycerol-3-Phosphate O-Acyltransferase
Dihydrolipoyllysine-Residue Acetyltransferase
Restriction Mapping
Promoter Regions, Genetic
Ribosomal Protein S6 Kinases
Hydro-Lyases
Transcription, Genetic
Recombinant Fusion Proteins
Brassica
Catalytic Domain
Mutagenesis, Site-Directed
Catalysis
Mass Spectrometry
Structure-Activity Relationship
Chloroplasts
Chromatography, High Pressure Liquid
Oxidoreductases
Acetyl-CoA C-Acetyltransferase
Streptomyces coelicolor
Hydrogen-Ion Concentration
Sequence Homology, Nucleic Acid
Chromatography, Gel
Phospholipids
Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase. (1/8)
Polyketides are a class of natural products that exhibit a wide range of functional and structural diversity. They include antibiotics, immunosuppressants, antifungals, antihypercholesterolemics, and cytotoxins. Polyketide synthases (PKSs) use chemistry similar to fatty acid synthases (FASs), although building block variation and differing extents of reduction of the growing polyketide chain underlie their biosynthetic versatility. In contrast to the well studied sequential modular type I PKSs, less is known about how the iterative type I PKSs carry out and control chain initiation, elongation, folding, and cyclization during polyketide processing. Domain structure analysis of a group of related fungal, nonreducing PKSs has revealed well defined N-terminal domains longer than commonly seen for FASs and modular PKSs. Predicted structure of this domain disclosed a region similar to malonyl-CoA:acyl-carrier protein (ACP) transacylases (MATs). MATs play a key role transferring precursor CoA thioesters from solution onto FASs and PKSs for chain elongation. On the basis of site-directed mutagenesis, radiolabeling, and kinetics experiments carried out with individual domains of the norsolorinic acid PKS, we propose that the N-terminal domain is a starter unit:ACP transacylase (SAT domain) that selects a C(6) fatty acid from a dedicated yeast-like FAS and transfers this unit onto the PKS ACP, leading to the production of the aflatoxin precursor, norsolorinic acid. These findings could indicate a much broader role for SAT domains in starter unit selection among nonreducing iterative, fungal PKSs, and they provide a biochemical rationale for the classical acetyl "starter unit effect." (+info)De novo fatty acid synthesis mediated by acyl-carrier protein in Neurospora crassa mitochondria. (2/8)
The acyl-carrier protein (ACP) in Neurospora crassa mitochondria [Brody, S. & Mikolajczyk, S. (1988) Eur. J. Biochem. 173, 353-359] mediated a cerulenin-sensitive, de novo fatty acid synthesis independent of the fatty acid synthetase complex present in the cytoplasm. Incubation of mitochondria with [2-14C]malonate labeled only the ACP as indicated by autoradiography after SDS/PAGE. Under these in vitro conditions ATP was required for the initial acyl-ACP formation, but further elongation required either magnesium or the direct addition of NADPH. Labeled hexanoic (6:0) and caprylic (8:0) acids were detected as intermediates in the pathway, as well as hydroxymyristic acid. All of the intermediates, and the eventual product of the reaction, myristic acid (14:0), were released from the ACP by alkaline treatment. Pulse-chase experiments demonstrated the incorporation on to, and release of label from, the ACP. In vivo labeling of ACP with [2-14C]malonate was also detected and the label was in the form of hydroxymyristic acid. This newly discovered pathway is discussed from the standpoint of its possible role in providing acyl chains for mitochondrial lipids. (+info)Purification and characterization of [acyl-carrier-protein] acetyltransferase from Escherichia coli. (3/8)
A multi-step procedure has been developed for the purification of [acyl-carrier-protein] acetyltransferase from Escherichia coli, which allows the production of small amounts of homogeneous enzyme. The subunit Mr was estimated to be 29,000 and the native Mr was estimated to be 61,000, suggesting a homodimeric structure. The catalytic properties of the enzyme are consistent with a Bi Bi Ping Pong mechanism and the existence of an acetyl-enzyme intermediate in the catalytic cycle. The enzyme was inhibited by N-ethylmaleimide and more slowly by iodoacetamide in reactions protected by the substrate, acetyl-CoA. However, the enzyme was apparently only weakly inhibited by the thiol-specific reagent methyl methanethiosulphonate. The nature of the acetyl-enzyme intermediate is discussed in relationship to that found in other similar enzymes from E. coli, yeast and vertebrates. (+info)Effect of thiolactomycin on the individual enzymes of the fatty acid synthase system in Escherichia coli. (4/8)
Thiolactomycin, an antibiotic with the structure of (4S)-(2E,5E)-2,4,6-trimethyl-3-hydroxy-2,5,7-octatriene-4-++ +thiolide, selectively inhibits type II fatty acid synthases. The mode of the thiolactomycin action on the fatty acid synthase system of Escherichia coli was investigated. Of the six individual enzymes of the fatty acid synthase system, [acyl-carrier-protein] (ACP) acetyltransferase and 3-oxoacyl-ACP synthase were inhibited by thiolactomycin. On the other hand, the other enzymes were not affected by this antibiotic. The thiolactomycin inhibition of the fatty acid synthase system was reversible. As to ACP acetyltransferase, the inhibition was competitive with respect to ACP and uncompetitive with respect to acetyl-CoA. As to 3-oxoacyl-ACP synthase, the inhibition was competitive with respect to malonyl-ACP and noncompetitive with respect to acetyl-ACP. The thiolactomycin action on the fatty acid synthase system was compared with that of cerulenin. (+info)Characterization of the fatty acid synthetase system of Curtobacterium pusillum. (5/8)
Curtobacterium pusillum contains 11-cyclohexylundecanoic acid as a major component of cellular fatty acids. A trace amount of 13-cyclohexyltridecanoic acid is also present. Fatty acids other than omega-cyclohexyl fatty acids present are 13-methyltetradecanoic, 12-methyltetradecanoic, n-pentadecanoic, 14-methylpentadecanoic, 13-methylpentadecanoic, n-hexadecanoic, 15-methylhexadecanoic, 14-methylhexadecanoic, and n-heptadecanoic acids. The fatty acid synthetase system of this bacterium was studied. Various 14C-labeled precursors were added to the growth medium and the incorporation of radioactivity into cellular fatty acids was analyzed. Sodium [14C]acetate and [14C]glucose were incorporated into almost all species of cellular fatty acids, the incorporation into 11-cyclohexylundecanoic acid being predominant. [14C]Isoleucine was incorporated into 12-methyltetradecanoic and 14-methylhexadecanoic acids: [14C]leucine into 13-methyltetradecanoic and 15-methylhexadecanoic acids; and [14C]valine into 14-methylpentadecanoic acid. [14C]-Shikimic acid was incorporated almost exclusively into omega-cyclohexyl fatty acids. The fatty acid synthetase activity of the crude enzyme preparation of C. pusillum was reconstituted on the addition of acyl carrier protein. This synthetase system required NADPH and preferentially utilized cyclohexanecarbonyl-CoA as a primer. The system was also able to use branched- and straight-chain acyl-CoAs with 4 to 6 carbon atoms effectively as primers but was unable to use acetyl-CoA. However, if acetyl acyl carrier protein was used as the priming substrate, the system produced straight-chain fatty acids. The results imply that the specificity of the initial acyl-CoA:acyl carrier protein acyltransferase dictates the structure of fatty acids synthesized and that the enzymes catalyzing the subsequent chain-elongation reactions do not have the same specificity restriction. (+info)Biochemical and genetic characterization of an auxotroph of Bacillus subtilis altered in the Acyl-CoA:acyl-carrier-protein transacylase. (6/8)
We have analyzed a mutation of Bacillus subtilis (bfmB) that results in an acyl-CoA:acyl-carrier-protein transacylase with low affinity for branched acyl-CoA substrates; it maps in the acf-hisH region of the chromosome. The aceA mutation, present in the parent of the bfmB mutant, causes a deficiency in pyruvate dehydrogenase and maps in the pycA-pyrA region. Strains carrying the bfmB mutation synthesize branched-chain fatty acids at a rate sufficient for normal growth only if branched acyl-CoA precursors are present in the medium. They grow well if the medium is supplemented with 0.1 mM 2-methylbutyrate, isobutyrate or isovalerate, or with 1.0 mM isoleucine or valine; leucine does not support growth. Growth supported by valine and isoleucine is inhibited by butyrate and other straight short-chain fatty acids at concentrations (0.1 mM) which do not inhibit growth of the standard strain; the inhibition is prevented by short branched fatty acids which are converted to long-chain fatty acids appearing as activity of B. subtilis is controlled by separate enzymatic sites for the acyl-CoA precursors of branched and straight-chain fatty acids. Whether these sites are contained in one or two enzymes is not known. (+info)The purification and function of acetyl coenzyme A:acyl carrier protein transacylase. (7/8)
When individual enzyme activities of the fatty acid synthetase (FAS) system were assayed in extracts from five different plant tissues, acetyl-CoA:acyl carrier protein (ACP) transacylase and beta-ketoacyl-ACP synthetases I and II had consistently low specific activities in comparison with the other enzymes of the system. However, two of these extracts synthesized significant levels of medium chain fatty acids (rather than C16 and C18 acid) from [14C]malonyl-CoA; these extracts had elevated levels of acetyl-CoA:ACP transacylase. To explore the role of the acetyl transacylase more carefully, this enzyme was purified some 180-fold from spinach leaf extracts. Varying concentrations of the transacylase were then added either to spinach leaf extracts or to a completely reconstituted FAS system consisting of highly purified enzymes. The results suggested that: (a) acetyl-CoA:ACP transacylase was the enzyme catalyzing the rate-limiting step in the plant FAS system; (b) increasing concentration of this enzyme markedly increased the levels of the medium chain fatty acids, whereas increase of the other enzymes of the FAS system led to increased levels of stearic acid synthesis; and (c) beta-ketoacyl-ACP synthetase I was not involved in the rate-limiting step. It is suggested that modulation of the activity of acetyl-CoA:ACP transacylase may have important implications in the type of fatty acid synthesized, as well as the amount of fatty acids formed. (+info)Beta-lactams SB 212047 and SB 216754 are irreversible, time-dependent inhibitors of coenzyme A-independent transacylase. (8/8)
The enzyme coenzyme A-independent transacylase (CoA-IT) has been demonstrated to be the key mediator of arachidonate remodeling, a process that moves arachidonate into 1-ether-containing phospholipids. Blockade of CoA-IT by reversible inhibitors has been shown to block the release of arachidonate in stimulated neutrophils and inhibit the production of eicosanoids and platelet-activating factor. We describe novel inhibitors of CoA-IT activity that contain a beta-lactam nucleus. beta-Lactams were investigated as potential mechanism-based inhibitors of CoA-IT on the basis of the expected formation of an acyl-enzyme intermediate complex. Two beta-lactams, SB 212047 and SB 216754, were shown to be specific, time-dependent inhibitors of CoA-IT activity (IC50 = 6 and 20 microM, respectively, with a 10-min pretreatment time). Extensive washing and dilution could not remove the inhibition, suggesting it was irreversible. In stimulated human monocytes, SB 216754 decreased the production of eicosanoids in a time-dependent manner. In an in vivo model of phorbol ester-induced ear inflammation, SB 216754 was able to inhibit indices of both edema and cell infiltration. Taken together, the results support two hypotheses: 1) CoA-IT activity is important for the production of inflammatory lipid mediators in stimulated cells and in vivo and 2) the mechanism by which CoA-IT acts to transfer arachidonate is through an acyl-enzyme intermediate. (+info)Protein S is a vitamin K-dependent protein that is produced in the liver and circulates in the blood. It works by inhibiting the activity of thrombin, a clotting factor that helps to form blood clots. In people with protein S deficiency, there may be an overactivation of thrombin, leading to an increased risk of blood clots forming.
Protein S deficiency can be caused by several factors, including genetic mutations, vitamin K deficiency, and certain medical conditions such as liver disease or cancer. It is usually diagnosed through a combination of clinical evaluation, laboratory tests, and imaging studies.
Treatment for protein S deficiency typically involves replacing the missing protein with intravenous immune globulin (IVIG) or recombinant human protein S. In some cases, medications that inhibit thrombin activity, such as heparins or direct thrombin inhibitors, may also be used to reduce the risk of blood clots forming.
Preventing protein S deficiency involves ensuring adequate intake of vitamin K through dietary sources or supplements, managing underlying medical conditions, and avoiding factors that can increase the risk of bleeding or thrombosis, such as smoking, obesity, and inactivity.
In summary, protein S deficiency is a condition characterized by low levels of protein S, which increases the risk of developing blood clots. It can be caused by several factors and treated with replacement therapy or medications that inhibit thrombin activity. Prevention involves ensuring adequate vitamin K intake and managing underlying medical conditions.
acyl-carrier-protein) S-acetyltransferase
Annonacin
Curacin A
Fatty-acyl-CoA synthase
UDP-3-O-(3-hydroxymyristoyl)glucosamine N-acyltransferase
Rubellin B
List of MeSH codes (D08)
Fatty acid synthase
Enterococcus faecalis
Thiolase
List of EC numbers (EC 2)
List of EC numbers (EC 4)
ACAT1
Chromosome 11
List of enzymes
Glucosamine-phosphate N-acetyltransferase
List of EC numbers (EC 1)
Carnitine palmitoyltransferase II deficiency
Pyruvate dehydrogenase complex
Platelet-activating factor
DeCS
Positive mood-related gut microbiota in a long-term closed environment: a multiomics study based on the "Lunar Palace 365"...
DeCS 2017 - December 21, 2017 version
Leveduras/metabolismo
MMTB
Antibiotics in the clinical pipeline in 2011 | The Journal of Antibiotics
Network Portal - Gene BC2209
"sequence id","alias","species","description",...
BiGG Metabolite coa c in iNRG857 1313
T3DB: Lead arsenite
Enzymes Biotechnology Handbook
SAUSA300 1133 - AureoWiki
nucleoside bisphosphate biosynthetic process - Ontology Report - Rat Genome Database
Category:E. coli complexes - EcoliWiki
Chromosome 11 (human) - wikidoc
Gene locus Report for: bovin-q3t0r6
"sequence id","alias","species","description",...
RegenerativeMedicine.net - Article Archives
SAB AP71658 Recombinant human-Viv体育(中国)有限公司
CoP: Co-expressed Biological Processes
Publications
GSE9006 HEALTHY VS TYPE 2 DIABETES PBMC AT DX DN
MH DELETED MN ADDED MN
EurekaMag PDF full texts Chapter 6194
Transacylase1
- Identification of a starter unit acyl-carrier protein transacylase domain in an iterative type I polyketide synthase. (nih.gov)
Enzymes4
- protein_coding" "AAC75228","fruA","Escherichia coli","fused fructose-specific PTS enzymes: IIBcomponent/IIC components [Ensembl]. (ntu.edu.sg)
- protein_coding" "AAC75230","fruB","Escherichia coli","fused fructose-specific PTS enzymes: IIA component/HPr component [Ensembl]. (ntu.edu.sg)
- With time, research, and improved protein engineering methods, many enzymes have been genetically modified to be more effective at the desired temperatures, pH, or under other manufacturing conditions typically inhibitory to enzyme activity (e.g. harsh chemicals), making them more suitable and efficient for industrial or home applications. (entrepreneurindia.co)
- This book basically deals with principles of industrial enzymology, basis of utilization of soluble and immobilized, enzymes in industrial processes, principles of immobilization of enzymes, enzymes in clinical analysis principles, practical aspects of large-scale protein purification, the applications of enzymes in industry, use of enzymes in the extraction of natural products, data on techniques of enzyme immobilization and bio affinity procedures etc. (entrepreneurindia.co)
Transmembrane1
- AP70858 Recombinant human Transmembrane protein 141 11055 6930 4125 2508 1452 0 1012 E.coli HUMAN GST-tag Store at -20°C, for extended storage, conserve at -20°C or -80°C. Repeated freezing and thawing is not recommended. (thesixteendigital.com)
Lysine2
- Probe Set ID Ref Seq Protein ID Signal Strength Name Gene Symbol Species Function Swiss-Prot ID Amino Acid Sequence 1367452_at NP_598278 16.52 small ubiquitin-related modifier 2 precursor Sumo2 Rattus norvegicus " Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. (nih.gov)
- This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. (nih.gov)
Eukaryotes1
- HN - 2006(1981) BX - Actin-Capping Proteins MH - Actin Depolymerizing Factors UI - D051339 MN - D5.750.78.730.212 MN - D12.776.220.525.212 MS - A family of low MOLECULAR WEIGHT actin-binding proteins found throughout eukaryotes. (nih.gov)
Binds3
- Arp2-3 complex binds WASP PROTEIN and existing ACTIN FILAMENTS, and it nucleates the formation of new branch point filaments. (nih.gov)
- HN - 2006 BX - Arp2-3 Complex MH - Actin-Related Protein 3 UI - D051378 MN - D5.750.78.730.246.750 MN - D12.776.220.525.246.750 MS - A component of the Arp2-3 complex that is related in sequence and structure to ACTIN and that binds ATP. (nih.gov)
- The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. (nih.gov)
Catalyzes3
- A enzyme that catalyzes the transfer of acetyl groups from ACETYL CoA to acyl-carrier protein to form COENZYME A and acetyl-acyl-carrier protein. (nih.gov)
- 9/3/2005) TOTAL DESCRIPTORS = 935 MH - 1-Acylglycerol-3-Phosphate O-Acyltransferase UI - D051103 MN - D8.811.913.50.173 MS - An enzyme that catalyzes the acyl group transfer of ACYL COA to 1-acyl-sn-glycerol 3-phosphate to generate 1,2-diacyl-sn-glycerol 3-phosphate. (nih.gov)
- An enzyme is a protein that catalyzes, or speeds up, a chemical reaction. (entrepreneurindia.co)
Substrate1
- LysR substrate binding domain, Bacterial regulatory helix-turn-helix protein [Interproscan]. (ntu.edu.sg)
Actin3
- AN - coordinate IM with ADENOMA (IM) HN - 2006 BX - Corticotroph Adenoma BX - Pituitary Adenoma, ACTH-Secreting BX - Pituitary Corticotropin-Secreting Adenoma MH - Actin Capping Proteins UI - D051344 MN - D5.750.78.730.32 MN - D12.776.220.525.32 MS - Actin capping proteins are cytoskeletal proteins that bind to the ends of ACTIN FILAMENTS to regulate actin polymerization. (nih.gov)
- HN - 2006(1981) BX - Cofilins MH - Actin-Related Protein 2 UI - D051377 MN - D5.750.78.730.246.500 MN - D12.776.220.525.246.500 MS - A PROFILIN binding domain protein that is part of the Arp2-3 complex. (nih.gov)
- HN - 2006(1998) MH - Actin-Related Protein 2-3 Complex UI - D051376 MN - D5.750.78.730.246 MN - D12.776.220.525.246 MS - A complex of seven proteins including ARP2 PROTEIN and ARP3 PROTEIN that plays an essential role in maintenance and assembly of the CYTOSKELETON. (nih.gov)
Subunit1
- protein_coding" "AAC73960","hcp","Escherichia coli","hybrid-cluster [4Fe-2S-2O] subunit of anaerobic terminal reductases [Ensembl]. (ntu.edu.sg)
Similarity3
- genome assembly, based on nucleotide similarity to the FAS proteins (tBLASTn) of humans, other mosquitoes and invertebrates. (biomedcentral.com)
- Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (By similarity). (nih.gov)
- Regulates E3 ubiquitin-protein ligase activity of RNF19A (By similarity). (nih.gov)
Abhydrolase1
- Bos mutus (wild yak) abhydrolase domain-containing protein 8 (EC 3. (inrae.fr)
Gene2
- So CCDS's gene number prediction represents a lower bound on the total number of human protein-coding genes. (wikidoc.org)
- AP70865 Recombinant Human Tumor necrosis factor-inducible gene 6 protein 11055 6930 4125 2508 1452 0 1012 E.coli HUMAN GST-tag Store at -20°C, for extended storage, conserve at -20°C or -80°C. Repeated freezing and thawing is not recommended. (thesixteendigital.com)
Copper1
- Copper resistance protein D [Interproscan]. (ntu.edu.sg)
Domain2
Complex2
- Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. (nih.gov)
- adaptor related protein complex 3 subu. (gsea-msigdb.org)
Unknown function3
- Protein of unknown function (DUF1158) [Interproscan]. (ntu.edu.sg)
- Protein of unknown function (DUF441) [Interproscan]. (ntu.edu.sg)
- Protein of unknown function (DUF2511) [Interproscan]. (ntu.edu.sg)
Human1
- Subretinal vector injections led to nearly complete suppression of endogenous canine RHO RNA, while the human RHO replacement cDNA resulted in up to 30% of normal RHO protein levels. (regenerativemedicine.net)
Biosynthesis1
- PcaA, MmaA4, Msh, Fad, Pim, PapA5 and MmpL7 proteins) participating in the biosynthesis of cell wall components with extremely tight and rigid structures are promising targets for new drugs against MTB, which can survive and grow in host macrophages via the aid of its strong cell wall. (medscape.com)
Cellular2
- the other components constitute the other major biochemical constituents of a cell such as the actual DNA sequence, protein levels, and cellular substructures. (nih.gov)
- This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. (nih.gov)
Gene3
- In the absence of full proteomic data (both primary proteins and modified proteins), it is valuable to understand the quantitative relationship between genes, which we will refer to as gene expression networks. (nih.gov)
- Probe Set ID Ref Seq Protein ID Signal Strength Name Gene Symbol Species Function Swiss-Prot ID Amino Acid Sequence 1367452_at NP_598278 7.9 small ubiquitin-related modifier 2 precursor Sumo2 Rattus norvegicus " Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. (nih.gov)
- RS is related to various mutations on the MECP2 gene, which codes for methyl-CpG binding protein-2 (MECP2). (medscape.com)
Structural1
- Icl, AceA and GlcB proteins) are useful targets for the structural design of agents active against both persistent and dormant types of MTB. (medscape.com)
Family2
- We focus specifically on two diseases: very long-chain acyl-CoA dehydrogenase deficiency (VLCADD) and malonyl-CoA synthetase deficiency (acyl-CoA synthetase family member 3 (ACSF3)) deficiency, which are both characterized by alterations in metabolic flexibility. (nih.gov)
- HN - 2006(1981) BX - Actin-Capping Proteins MH - Actin Depolymerizing Factors UI - D051339 MN - D5.750.78.730.212 MN - D12.776.220.525.212 MS - A family of low MOLECULAR WEIGHT actin-binding proteins found throughout eukaryotes. (nih.gov)
Signal1
- Polymeric SUMO2 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins (By similarity). (nih.gov)
Activity1
- Regulates E3 ubiquitin-protein ligase activity of RNF19A (By similarity). (nih.gov)
Levels1
- It is expressed at higher levels than ARP2 PROTEIN and does not contain a PROFILIN binding domain. (nih.gov)