Related Research Articles
Arginine is the amino acid with the formula (H2N)(HN)CN(H)(CH2)3CH(NH2)CO2H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO2−) and both the amino and guanidino groups are protonated, resulting in a cation. Only the l-arginine (symbol Arg or R) enantiomer is found naturally. Arg residues are common components of proteins. It is encoded by the codons CGU, CGC, CGA, CGG, AGA, and AGG. The guanidine group in arginine is the precursor for the biosynthesis of nitric oxide. Like all amino acids, it is a white, water-soluble solid.
The organic compound citrulline is an α-amino acid. Its name is derived from citrullus, the Latin word for watermelon. Although named and described by gastroenterologists since the late 19th century, it was first isolated from watermelon in 1914 by Japanese researchers Yotaro Koga and Ryo Odake and further codified by Mitsunori Wada of Tokyo Imperial University in 1930. It has the formula H2NC(O)NH(CH2)3CH(NH2)CO2H. It is a key intermediate in the urea cycle, the pathway by which mammals excrete ammonia by converting it into urea. Citrulline is also produced as a byproduct of the enzymatic production of nitric oxide from the amino acid arginine, catalyzed by nitric oxide synthase.
In the mitochondrion, the matrix is the space within the inner membrane. The word "matrix" stems from the fact that this space is viscous, compared to the relatively aqueous cytoplasm. The mitochondrial matrix contains the mitochondrial DNA, ribosomes, soluble enzymes, small organic molecules, nucleotide cofactors, and inorganic ions.[1] The enzymes in the matrix facilitate reactions responsible for the production of ATP, such as the citric acid cycle, oxidative phosphorylation, oxidation of pyruvate, and the beta oxidation of fatty acids.
Lysinuric protein intolerance (LPI) is an autosomal recessive metabolic disorder affecting amino acid transport.
The Transporter Classification Database is an International Union of Biochemistry and Molecular Biology (IUBMB)-approved classification system for membrane transport proteins, including ion channels.
An amino acid transporter is a membrane transport protein that transports amino acids. They are mainly of the solute carrier family.
The mercury transporter superfamily is a family of transmembrane bacterial transporters of mercury ions. The common origin of all Mer superfamily members has been established. The common elements between family members are included in TMSs 1-2. A representative list of the subfamilies and proteins that belong to those subfamilies is available in the Transporter Classification Database.
The lysosomal cystine transporter (LCT) family is part of the TOG Superfamily and includes secondary transport proteins that are derived from animals, plants, fungi and other eukaryotes. They exhibit 7 putative transmembrane α-helical spanners (TMSs) and vary in size between about 200 and 500 amino acyl residues, although most have between 300 and 400 residues.
The amino acid-polyamine-organocation (APC) superfamily is the second largest superfamily of secondary carrier proteins currently known, and it contains several Solute carriers. Originally, the APC superfamily consisted of subfamilies under the transporter classification number. This superfamily has since been expanded to include eighteen different families.
The Amino Acid-Polyamine-Organocation (APC) Family of transport proteins includes members that function as solute:cation symporters and solute:solute antiporters. They occur in bacteria, archaea, fungi, unicellular eukaryotic protists, slime molds, plants and animals. They vary in length, being as small as 350 residues and as large as 850 residues. The smaller proteins are generally of prokaryotic origin while the larger ones are of eukaryotic origin. Most of them possess twelve transmembrane α-helical spanners but have a re-entrant loop involving TMSs 2 and 3. The APC Superfamily was established to encompass a wider range of homologues.
Lysine Exporters are a superfamily of transmembrane proteins which export amino acids, lipids and heavy metal ions. They provide ionic homeostasis, play a role in cell envelope assembly, and protect from excessive concentrations of heavy metals in cytoplasm. The superfamily was named based on the early discovery of the LysE carrier protein of Corynebacterium glutamicum.
Divalent anion:Na+ symporters were found in bacteria, archaea, plant chloroplasts and animals.
The p-aminobenzoyl-glutamate transporter(AbgT) family is a family of transporter proteins belonging to the ion transporter (IT) superfamily. The AbgT family consists of the AbgT protein of E. coli and the MtrF drug exporter of Neisseria gonorrhoeae. The former protein is apparently cryptic in wild-type cells, but when expressed on a high copy number plasmid, or when expressed at higher levels due to mutation, it appeared to allow uptake and subsequent utilization of p-aminobenzoyl-glutamate as a source of p-aminobenzoate for p-aminobenzoate auxotrophs. p-Aminobenzoate is a constituent of and a precursor for the biosynthesis of folic acid. MtrF was annotated as a putative drug efflux pump.
The ion transporter (IT) superfamily is a superfamily of secondary carriers that transport charged substrates.
The C4-dicarboxylate uptake family or Dcu family is a family of transmembrane ion transporters found in bacteria. Their function is to exchange dicarboxylates such as aspartate, malate, fumarate and succinate.
The arsenical resistance-3 (ACR3) family is a member of the BART superfamily. Based on operon analyses, ARC3 homologues may function either as secondary carriers or as primary active transporters, similarly to the ArsB and ArsAB families. In the latter case ATP hydrolysis again energizes transport. ARC3 homologues transport the same anions as ArsA/AB homologues, though ArsB homologues are members of the IT Superfamily and homologues of the ARC3 family are within the BART Superfamily suggesting they may not be evolutionarily related.
The Malonate Uptake (MatC) family is a constituent of the ion transporter (IT) superfamily. It consists of proteins from Gram-negative and Gram-positive bacteria, simple eukaryotes and archaea. The proteins are of about 450 amino acyl residues in length with 12-14 putative transmembrane segments (TMSs). Closest functionally-characterized homologues are in the DASS family. One member of this family is a putative malonate transporter.
The NhaC family belongs to the Ion Transporter (IT) Superfamily. A representative list of proteins belonging to the NhaC family can be found in the Transporter Classification Database.
The NhaE family belongs to the Ion Transporter (IT) Superfamily, which has an end. A representative list of proteins belonging to the NhaE family can be found in the Transporter Classification Database.
The Cation:Proton Antiporter (CPA) Superfamily is a superfamily of transport proteins named after one of its constituent members, the monovalent cation:proton antiporter-2.
References
- ↑ Lolkema, Juke S.; Slotboom, Dirk Jan (2003-04-11). "Classification of 29 families of secondary transport proteins into a single structural class using hydropathy profile analysis" (PDF). Journal of Molecular Biology. 327 (5): 901–909. doi:10.1016/s0022-2836(03)00214-6. ISSN 0022-2836. PMID 12662917.
- ↑ Prakash, Shraddha; Cooper, Garret; Singhi, Soumya; Saier, Milton H. (2003-12-03). "The ion transporter superfamily". Biochimica et Biophysica Acta (BBA) - Biomembranes. 1618 (1): 79–92. doi: 10.1016/j.bbamem.2003.10.010 . ISSN 0006-3002. PMID 14643936.
- ↑ Rabus, R.; Jack, D. L.; Kelly, D. J.; Saier, M. H. (1999-12-01). "TRAP transporters: an ancient family of extracytoplasmic solute-receptor-dependent secondary active transporters". Microbiology. 145 ( Pt 12) (12): 3431–3445. doi: 10.1099/00221287-145-12-3431 . ISSN 1350-0872. PMID 10627041.
- ↑ Gupta, Radha; Yang, Jun; Dong, Yimin; Swiatlo, Edwin; Zhang, Jing-Ren; Metzger, Dennis W.; Bai, Guangchun (2013-10-01). "Deletion of arcD in Streptococcus pneumoniae D39 impairs its capsule and attenuates virulence". Infection and Immunity. 81 (10): 3903–3911. doi:10.1128/IAI.00778-13. ISSN 1098-5522. PMC 3811789 . PMID 23918778.
- ↑ Rimaux, Tom; Rivière, Audrey; Hebert, Elvira María; Mozzi, Fernanda; Weckx, Stefan; De Vuyst, Luc; Leroy, Frédéric (2013-04-01). "A putative transport protein is involved in citrulline excretion and re-uptake during arginine deiminase pathway activity by Lactobacillus sakei". Research in Microbiology. 164 (3): 216–225. doi:10.1016/j.resmic.2012.11.004. ISSN 1769-7123. PMID 23178175.
As of this edit, this article uses content from "2.A.118 The Basic Amino Acid Antiporter (ArcD) Family" , which is licensed in a way that permits reuse under the Creative Commons Attribution-ShareAlike 3.0 Unported License, but not under the GFDL. All relevant terms must be followed.
 | This membrane protein–related article is a stub. You can help Wikipedia by expanding it. |