YedZ family

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YedZ (TC# 5.B.7) of E. coli has been examined topologically and has 6 transmembrane segments (TMSs) with both the N- and C-termini localized to the cytoplasm. [1] von Rozycki et al. 2004 identified homologues of YedZ in bacteria and animals. YedZ homologues exhibit conserved histidyl residues in their transmembrane domains that may function in heme binding. [2] Some of the homologues encoded in the genomes of various bacteria have YedZ domains fused to transport, electron transfer and biogenesis proteins. [2] One of the animal homologues is the 6 TMS epithelial plasma membrane antigen of the prostate (STAMP1) that is over-expressed in prostate cancer. Some animal homologues have YedZ domains fused C-terminal to homologues of NADP oxidoreductases.

YedZ homologues arose by intragenic triplication of a 2 TMS-encoding element. They exhibit statistically significant sequence similarity to two families of putative heme export systems and one family of cytochrome-containing electron carriers and have biogenesis. [2] YedZ homologues can function as heme-binding proteins that facilitate or regulate oxidoreduction, transmembrane electron flow and transport. Homologues of YedZ are found in a variety of bacteria, including magnetotactic bacteria and cyanobacteria where YedZ domains are fused C-terminal to magnetosome transporters of the MFS superfamily (TC# 2.A.1) and to electron carriers of the DsbD family (TC# 5.A.1), respectively.

YedZ homologues are found in animals where one includes a human 6 TMS epithelial plasma membrane antigen that is expressed at high levels in prostate cancer cells. [3] [4] Even more distant homologues may include the transmembrane domain within members of the gp91phoxNADPH oxidase associated cytochrome b558 (CytB) family (TC #5.B.2). Heme-containing transmembrane ferric reductase domains (FRD) are found in both bacterial and eukaryotic proteins including ferric reductases (FRE), and NADPH oxidases (NOX). [2] Bacteria contain FRD proteins consisting only of a ferric reductase domain, such as YedZ and short FRE proteins. Full length FRE and NOX enzymes are mostly found in eukaryotes and possess a dehydrogenase domain, allowing them to catalyze electron transfer from cytosolic NADPH to extracellular metal ions (FRE) or oxygen (NOX). Metazoa possess YedZ-related STEAP proteins. Phylogenetic analyses suggests that FRE enzymes appeared early in evolution, followed by a transition towards EF-hand containing NOX enzymes (NOX5- and DUOX-like). NOX enzymes are distinguished from FRE enzymes through a four amino acid motif spanning from transmembrane domain 3 (TM3) to TM4, and YedZ/STEAP proteins are identified by the replacement of the first canonical heme-spanning histidine by a highly conserved arginine. [5]

Six-transmembrane epithelial antigen of the prostate 3 (Steap3) is the major ferric reductase in developing erythrocytes. Steap family proteins are defined by a shared transmembrane domain that in Steap3 has been shown to function as a transmembrane electron shuttle, moving cytoplasmic electrons derived from NADPH across the lipid bilayer to the extracellular face where they are used to reduce Fe3+ to Fe2+ and potentially Cu2+ to Cu1+. [6] High affinity FAD and iron binding sites and a single b-type heme binding site is present in the Steap3 transmembrane domain. Steap3 is functional as a homodimer and utilizes an intrasubunit electron transfer pathway through the single heme moiety rather than an intersubunit electron pathway through a potential domain-swapped dimer. [6] The sequence motifs in the transmembrane domain that are associated with the FAD and metal binding sites are not only present in Steap2 and Steap4 but also in Steap1 which lacks the N-terminal oxidoreductase domain, suggesting that Steap1 harbors latent oxidoreductase activity.

Related Research Articles

In biochemistry, an oxidoreductase is an enzyme that catalyzes the transfer of electrons from one molecule, the reductant, also called the electron donor, to another, the oxidant, also called the electron acceptor. This group of enzymes usually utilizes NADP+ or NAD+ as cofactors. Transmembrane oxidoreductases create electron transport chains in bacteria, chloroplasts and mitochondria, including respiratory complexes I, II and III. Some others can associate with biological membranes as peripheral membrane proteins or be anchored to the membranes through a single transmembrane helix.

<span class="mw-page-title-main">Nitric oxide synthase</span> Enzyme catalysing the formation of the gasotransmitter NO(nitric oxide)

Nitric oxide synthases (NOSs) are a family of enzymes catalyzing the production of nitric oxide (NO) from L-arginine. NO is an important cellular signaling molecule. It helps modulate vascular tone, insulin secretion, airway tone, and peristalsis, and is involved in angiogenesis and neural development. It may function as a retrograde neurotransmitter. Nitric oxide is mediated in mammals by the calcium-calmodulin controlled isoenzymes eNOS and nNOS. The inducible isoform, iNOS, involved in immune response, binds calmodulin at physiologically relevant concentrations, and produces NO as an immune defense mechanism, as NO is a free radical with an unpaired electron. It is the proximate cause of septic shock and may function in autoimmune disease.

<span class="mw-page-title-main">Nicotinamide adenine dinucleotide phosphate</span> Chemical compound

Nicotinamide adenine dinucleotide phosphate, abbreviated NADP+ or, in older notation, TPN (triphosphopyridine nucleotide), is a cofactor used in anabolic reactions, such as the Calvin cycle and lipid and nucleic acid syntheses, which require NADPH as a reducing agent ('hydrogen source'). NADPH is the reduced form, whereas NADP+ is the oxidized form. NADP+ is used by all forms of cellular life.

Ferredoxins are iron–sulfur proteins that mediate electron transfer in a range of metabolic reactions. The term "ferredoxin" was coined by D.C. Wharton of the DuPont Co. and applied to the "iron protein" first purified in 1962 by Mortenson, Valentine, and Carnahan from the anaerobic bacterium Clostridium pasteurianum.

<span class="mw-page-title-main">Biliverdin reductase</span> Class of enzymes

Biliverdin reductase (BVR) is an enzyme found in all tissues under normal conditions, but especially in reticulo-macrophages of the liver and spleen. BVR facilitates the conversion of biliverdin to bilirubin via the reduction of a double-bond between the second and third pyrrole ring into a single-bond.

<span class="mw-page-title-main">Vitamin K epoxide reductase</span> Class of enzymes

Vitamin K epoxide reductase (VKOR) is an enzyme that reduces vitamin K after it has been oxidised in the carboxylation of glutamic acid residues in blood coagulation enzymes. VKOR is a member of a large family of predicted enzymes that are present in vertebrates, Drosophila, plants, bacteria and archaea. In some plant and bacterial homologues, the VKOR domain is fused with domains of the thioredoxin family of oxidoreductases.

<span class="mw-page-title-main">Cytochrome P450 reductase</span> Mammalian protein found in Homo sapiens

Cytochrome P450 reductase is a membrane-bound enzyme required for electron transfer from NADPH to cytochrome P450 and other heme proteins including heme oxygenase in the endoplasmic reticulum of the eukaryotic cell.

<span class="mw-page-title-main">Formate dehydrogenase</span>

Formate dehydrogenases are a set of enzymes that catalyse the oxidation of formate to carbon dioxide, donating the electrons to a second substrate, such as NAD+ in formate:NAD+ oxidoreductase (EC 1.17.1.9) or to a cytochrome in formate:ferricytochrome-b1 oxidoreductase (EC 1.2.2.1). This family of enzymes has attracted attention as inspiration or guidance on methods for the carbon dioxide fixation, relevant to global warming.

<span class="mw-page-title-main">Protochlorophyllide reductase</span>

In enzymology, protochlorophyllide reductases (POR) are enzymes that catalyze the conversion from protochlorophyllide to chlorophyllide a. They are oxidoreductases participating in the biosynthetic pathway to chlorophylls.

In enzymology, a ferredoxin-NADP+ reductase (EC 1.18.1.2) abbreviated FNR, is an enzyme that catalyzes the chemical reaction

In enzymology, a ferric-chelate reductase (EC 1.16.1.7) is an enzyme that catalyzes the chemical reaction

Flavin reductase a class of enzymes. There are a variety of flavin reductases, which bind free flavins and through hydrogen bonding, catalyze the reduction of these molecules to a reduced flavin. Riboflavin, or vitamin B, and flavin mononucleotide are two of the most well known flavins in the body and are used in a variety of processes which include metabolism of fat and ketones and the reduction of methemoglobin in erythrocytes. Flavin reductases are similar and often confused for ferric reductases because of their similar catalytic mechanism and structures.

<span class="mw-page-title-main">Thiosulfate dehydrogenase</span>

Thiosulfate dehydrogenase is an enzyme that catalyzes the chemical reaction:

<span class="mw-page-title-main">Dual oxidase 1</span> Protein-coding gene in the species Homo sapiens

Dual oxidase 1, also known as DUOX1 or ThOX1, is an enzyme which in humans is encoded by the DUOX1 gene. DUOX1 was first identified in the mammalian thyroid gland. In humans, two isoforms are found; hDUOX1 and hDUOX2. Human DUOX protein localization is not exclusive to thyroid tissue; hDUOX1 is prominent in airway epithelial cells and hDUOX2 in the salivary glands and gastrointestinal tract.

<span class="mw-page-title-main">STEAP3</span> Protein-coding gene in the species Homo sapiens

Metalloreductase STEAP3 is an enzyme that in humans is encoded by the STEAP3 gene.

<span class="mw-page-title-main">STEAP2</span> Protein-coding gene in the species Homo sapiens

Metalloreductase STEAP2 is an enzyme that in humans is encoded by the STEAP2 gene.

<span class="mw-page-title-main">Fumarate reductase (quinol)</span>

Fumarate reductase (quinol) (EC 1.3.5.4, QFR,FRD, menaquinol-fumarate oxidoreductase, quinol:fumarate reductase) is an enzyme with systematic name succinate:quinone oxidoreductase. This enzyme catalyzes the following chemical reaction:

Adrenodoxin-NADP+ reductase (EC 1.18.1.6, adrenodoxin reductase, nicotinamide adenine dinucleotide phosphate-adrenodoxin reductase, ADR, NADPH:adrenal ferredoxin oxidoreductase) is an enzyme with systematic name adrendoxin:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Biliverdin reductase B</span> Protein-coding gene in the species Homo sapiens

Biliverdin reductase B is a protein that in humans is encoded by the BLVRB gene.

The Disulfide bond oxidoreductase D (DsbD) family is a member of the Lysine Exporter (LysE) Superfamily. A representative list of proteins belonging to the DsbD family can be found in the Transporter Classification Base.

References

  1. ↑ Drew, David; Sjöstrand, Dan; Nilsson, Johan; Urbig, Thomas; Chin, Chen-ni; de Gier, Jan-Willem; von Heijne, Gunnar (2002-03-05). "Rapid topology mapping of Escherichia coli inner-membrane proteins by prediction and PhoA/GFP fusion analysis". Proceedings of the National Academy of Sciences of the United States of America. 99 (5): 2690–2695. Bibcode:2002PNAS...99.2690D. doi: 10.1073/pnas.052018199 . ISSN   0027-8424. PMC   122409 . PMID   11867724.
  2. 1 2 3 4 von Rozycki, Torsten; Yen, Ming-Ren; Lende, Erik E.; Saier, Milton H. (2004-01-01). "The YedZ family: possible heme binding proteins that can be fused to transporters and electron carriers". Journal of Molecular Microbiology and Biotechnology. 8 (3): 129–140. doi:10.1159/000085786. ISSN   1464-1801. PMID   16088215. S2CID   34128668.
  3. ↑ Hubert, R. S.; Vivanco, I.; Chen, E.; Rastegar, S.; Leong, K.; Mitchell, S. C.; Madraswala, R.; Zhou, Y.; Kuo, J. (1999-12-07). "STEAP: a prostate-specific cell-surface antigen highly expressed in human prostate tumors". Proceedings of the National Academy of Sciences of the United States of America. 96 (25): 14523–14528. Bibcode:1999PNAS...9614523H. doi: 10.1073/pnas.96.25.14523 . ISSN   0027-8424. PMC   24469 . PMID   10588738.
  4. ↑ Yang, D.; Holt, G. E.; Velders, M. P.; Kwon, E. D.; Kast, W. M. (2001-08-01). "Murine six-transmembrane epithelial antigen of the prostate, prostate stem cell antigen, and prostate-specific membrane antigen: prostate-specific cell-surface antigens highly expressed in prostate cancer of transgenic adenocarcinoma mouse prostate mice". Cancer Research. 61 (15): 5857–5860. ISSN   0008-5472. PMID   11479226.
  5. ↑ Zhang, Xuezhi; Krause, Karl-Heinz; Xenarios, Ioannis; Soldati, Thierry; Boeckmann, Brigitte (2013-01-01). "Evolution of the ferric reductase domain (FRD) superfamily: modularity, functional diversification, and signature motifs". PLOS ONE. 8 (3): e58126. Bibcode:2013PLoSO...858126Z. doi: 10.1371/journal.pone.0058126 . ISSN   1932-6203. PMC   3591440 . PMID   23505460.
  6. 1 2 Kleven, Mark D.; Dlakić, Mensur; Lawrence, C. Martin (2015-09-11). "Characterization of a single b-type heme, FAD, and metal binding sites in the transmembrane domain of six-transmembrane epithelial antigen of the prostate (STEAP) family proteins". The Journal of Biological Chemistry. 290 (37): 22558–22569. doi: 10.1074/jbc.M115.664565 . ISSN   1083-351X. PMC   4566230 . PMID   26205815.

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