 | This article may be too technical for most readers to understand.(September 2016) |
The PTS Mannose-Fructose-Sorbose (Man) Family (TC# 4.A.6) is a group of multicomponent PTS systems that are involved in sugar uptake in bacteria. This transport process is dependent on several cytoplasmic phosphoryl transfer proteins - Enzyme I (I), HPr, Enzyme IIA (IIA), and Enzyme IIB (IIB) as well as the integral membrane sugar permease complex (IICD). It is not part of the PTS-AG or PTS-GFL superfamilies.
The Man Family is unique in several respects among other PTS porter families:
The mannose porter of Escherichia coli , for example, can transport and phosphorylate glucose, mannose, fructose, glucosamine, N-acetylglucosamine, and N-acteylmannosamine. [2]
The structure of the E. coli IIAMan domain has been shown to exhibit an α/β doubly wound superfold. [3] The IIB domain also exhibits an α/β doubly wound superfold, but it is very dissimilar from that of the IIA domain. [4] Instead, it has the same topology as phosphoglyceromutase (PGM). Since both proteins (IIBMan and PGM) catalyze phosphoryl transfer with a phosphohistidine intermediate, both proteins show a similar distribution of active site residues, and both exhibit similar structures, they are probably homologous.
IICMan of E. coli has been reported to have six transmembrane α-helical segments, while IIDMan was reported to have only one. [5] [6] However, hydropathy plots show multiple peaks of hydropathy, rendering the experimental result, suggesting 1 TMS, questionable. [7] These two proteins together are required for transport, although IICMan is presumed to comprise all or most of the sugar transporting channel.
The generalized reaction catalyzed by members of the Man Family is:
In chemistry, phosphorylation of a molecule is the attachment of a phosphoryl group. This process and its inverse, dephosphorylation, are critical for many cellular processes in biology. Protein phosphorylation is especially important for their function; for example, this modification activates almost half of the enzymes present in Saccharomyces cerevisiae, thereby regulating their function. Many proteins are phosphorylated temporarily, as are many sugars, lipids, and other biologically-relevant molecules.
Mannose is a sugar monomer of the aldohexose series of carbohydrates. It is a C-2 epimer of glucose. Mannose is important in human metabolism, especially in the glycosylation of certain proteins. Several congenital disorders of glycosylation are associated with mutations in enzymes involved in mannose metabolism.
PEP group translocation, also known as the phosphotransferase system or PTS, is a distinct method used by bacteria for sugar uptake where the source of energy is from phosphoenolpyruvate (PEP). It is known to be a multicomponent system that always involves enzymes of the plasma membrane and those in the cytoplasm.
Microcins are very small bacteriocins, composed of relatively few amino acids. For this reason, they are distinct from their larger protein cousins. The classic example is microcin V, of Escherichia coli. Subtilosin A is another bacteriocin from Bacillus subtilis. The peptide has a cyclized backbone and forms three cross-links between the sulphurs of Cys13, Cys7 and Cys4 and the alpha-positions of Phe22, Thr28 and Phe31.
The galactose permease or GalP found in Escherichia coli is an integral membrane protein involved in the transport of monosaccharides, primarily hexoses, for utilization by E. coli in glycolysis and other metabolic and catabolic pathways (3,4). It is a member of the Major Facilitator Super Family (MFS) and is homologue of the human GLUT1 transporter (4). Below you will find descriptions of the structure, specificity, effects on homeostasis, expression, and regulation of GalP along with examples of several of its homologues.
Phosphofructokinase (PFK) is a kinase enzyme that phosphorylates fructose 6-phosphate in glycolysis.
In enzymology, N-acetylglucosamine-6-phosphate deacetylase (EC 3.5.1.25), also known as GlcNAc-6-phosphate deacetylase or NagA, is an enzyme that catalyzes the deacetylation of N-acetylglucosamine-6-phosphate (GlcNAc-6-P) to glucosamine-6-phosphate (GlcN-6-P):
In enzymology, a protein-Npi-phosphohistidine-sugar phosphotransferase is an enzyme that catalyzes the chemical reaction
Phosphocarrier HPr protein is a small cytoplasmic protein that is a component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (PTS).
The bacterial phosphoenolpyruvate: sugar phosphotransferase system (PTS) is a multi-protein system involved in the regulation of a variety of metabolic and transcriptional processes. The PTS catalyzes the phosphorylation of incoming sugar substrates concomitant with their translocation across the cell membrane. The general mechanism of the PTS is the following: a phosphoryl group from phosphoenolpyruvate (PEP) is transferred to enzyme-I (EI) of PTS which in turn transfers it to a phosphoryl carrier protein (HPr). Phospho-HPr then transfers the phosphoryl group to a sugar-specific permease which consists of at least three structurally distinct domains which can either be fused together in a single polypeptide chain or exist as two or three interactive chains, formerly called enzymes II (EII) and III (EIII). The IIC domain catalyzes the transfer of a phosphoryl group from IIB to the sugar substrate.
Bacteriocin AS-48 is a cyclic peptide antibiotic produced by the eubacteria Enterococcus faecalis that shows a broad antimicrobial spectrum against both Gram-positive and Gram-negative bacteria. Bacteriocin AS-48 is encoded by the pheromone-responsive plasmid pMB2, and acts on the plasma membrane in which it opens pores leading to ion leakage and cell death. The globular structure of bacteriocin AS-48 is composed of five alpha helices enclosing a hydrophobic core. The mammalian NK-lysin effector protein of T and natural killer cells has a similar structure, though it lacks sequence homology with bacteriocins AS-48.
Proteins currently known to belong to the Ni2+-Co2+ Transporter (NiCoT) family (TC# 2.A.52) can be found in organisms ranging from Gram-negative and Gram-positive bacteria to archaea and some eukaryotes. Members of this family catalyze uptake of Ni2+ and/or Co2+ in a proton motive force-dependent process.
The phosphotransferases system (PTS-GFL) superfamily is a superfamily of phosphotransferase enzymes that facilitate the transport of glucose, glucitol (G), fructose (F) and lactose (L). Classification has been established through phylogenic analysis and bioinformatics.
The PTSGlucose-Glucoside (Glc) family includes porters specific for glucose, glucosamine, N-acetylglucosamine and a large variety of α- and β-glucosides, and is part of the PTS-GFL superfamily.
The PTS Fructose-Mannitol (Fru) Family is a large and complex family that is part of the PTS-GFL superfamily. It includes several sequenced fructose, mannose and mannitol-specific porters, as well as several putative PTS porters of unknown specificities. The fructose porters of this family phosphorylate fructose on the 1-position. Those of TC family 4.A.6 phosphorylate fructose on the 6-position.
The PTS Lactose-N,N’-Diacetylchitobiose (Lac) Family includes several sequenced lactose porters of Gram-positive bacteria, as well as the Escherichia coli and Borrelia burgdorferi N,N'-diacetylchitobiose (Chb) porters. It is part of the PTS-GFL superfamily. The former can transport aromatic β-glucosides and cellobiose, as well as Chb. However, only Chb induces expression of the chb operon.
The PTS Glucitol (Gut) Family consists only of glucitol-specific porters, but these occur both in Gram-negative and Gram-positive bacteria. It is part of the PTS-GFL superfamily.
Permease of phosphotransferase system is a superfamily of phosphotransferase enzymes that facilitate the transport of L-ascorbate (A) and galactitol (G). Classification has been established through phylogenic analysis and bioinformatics.
The PTS Galactitol (Gat) Family is part of the PTS-AG superfamily. The biochemistry of this family is poorly defined. The only well-characterized member of this family is the galactitol permease of Escherichia coli. However, a homologous IIC protein from Listeria monocytogenes has been shown to be required for D-arabitol fermentation. It presumably functions together with IIAGat and IIBGat homologues. IICGat is distantly related to IICSgc of E. coli; IIAGat is distantly related to IIASga and IIASgcof E. coli as well as IIAMtl and IIAFru. IIBGat is distantly related to IIBSga and IIBSgc of E. coli. Domains in the LicR/CelR family of transcriptional activators show C-terminal domains exhibiting weak sequence similarity to IIBGat and IIAGat.
The PTS L-Ascorbate (L-Asc) Family includes porters specific for L-ascorbate, and is part of the PTS-AG superfamily. A single PTS permease of the L-Asc family of PTS permeases has been functionally characterized. This is the SgaTBA system, renamed UlaABC by Yew and Gerlt.
As of this edit, this article uses content from "4.A.6 The PTS Mannose-Fructose-Sorbose (Man) 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.