| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
1 Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden
2 Stockholm Bioinformatics Centre, Karolinska Institutet, S-171 77 Stockholm, Sweden
Reprint requests to: Hans Jörnvall, Department of Medical Biochemistry and Biophysics, Karolinska Institutet, S-171 77 Stockholm, Sweden; e-mail: hans.jornvall{at}mbb.ki.se; fax: +46-8-337-462.
(RECEIVED July 3, 2001; FINAL REVISION November 30, 2001; ACCEPTED November 30, 2001)
Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.26902.
 |
Abstract |
|---|
 TOP Abstract IntroductionResults and DiscussionMaterials and methodsReferences |
|---|
Keywords: Short-chain dehydrogenases/reductases; human genome; cross-genome comparisons; orthologs; bioinformatics; steroid dehydrogenases
|
Introduction |
|---|
|
TOPAbstractIntroductionResults and DiscussionMaterials and methodsReferences |
|---|
Recent progress in genome characterizations has opened new routes for studies of this enzyme family. We have previously reported on the occurrence of SDR members in the bacterial and yeast genomes (Jörnvall et al. 1999). The availability of the human genome (International Human Genome Sequencing Consortium 2001; Venter et al. 2001) enabled us to find novel relationships. We have also extracted SDR members from the genomes of three model organisms (Caenorhabditis elegans, Drosophila melanogaster and Arabidopsis thaliana) and clustered the SDR sequences to define ortholog groups within this widespread enzyme family.
|
Results and Discussion |
|---|
|
TOPAbstractIntroductionResults and DiscussionMaterials and methodsReferences |
|---|
). The high number in A. thaliana is compatible with the tetraploidicity and gene multiplicity in that genome (Bancroft 2000). After reduction of close homologs (>60% residue identity in pairwise comparisons), the numbers do not vary much, but range from 56 to 62 (Table 1).
|
2000 open reading frames), in which only the extended forms are found (Jörnvall et al. 1999).
SDR forms occurring in all genomes
We have defined the orthologous forms of the human SDRs in the three model genomes of Drosophila melanogaster, Caenorhabditis elegans, and Arabidopsis thaliana. As a result of this search, we find eight SDR clusters present in all four genomes (Table 2, top). Of these, half are of the extended type, thus exceeding the ratio expected from the general distribution of human SDRs (13 extended clusters versus 34 classical clusters; Table 2). This emphasizes the ubiquitous occurrence of the extended SDRs, compatible with their presence also in genomes from unicellar organisms (Jörnvall et al. 1999).
|
The four generally occurring clusters with classical SDRs are represented by the human Hep27, FVT1, 17ß-HSD3, and WWOX structures. To date, the molecular function only of 17ß-HSD3 has been defined (Geissler et al. 1994). This enzyme is involved in tissue-specific testosterone synthesis and defects in its gene cause male pseudo-hermaphroditism. The corresponding SDR cluster (cluster 7 in Table 2
) is the second largest of all eight clusters, containing additional sequences: two from human, five from D. melanogaster, three from C. elegans, and two from A. thaliana. The defined function of 17ß-HSD3 indicates that these gene products are involved in tissue- and species-specific steroid metabolism.
The other three clusters of the classical type contain human enzymes with hitherto undefined functions. Hep27 is a nuclear protein with a restricted expression pattern and the corresponding cDNA was cloned from a hepatocarcinoma cell line (Gabrielli et al. 1995). This cluster also contains the human gene SRL (O95162 in Table 2), which codes for a peroxisomal SDR and displays 64% identity at the amino acid level towards Hep27 (Fransen et al. 1999). Similarly, the remaining two clusters, represented by FVT1 and WWOX, show involvement in malignant transformations. FVT1 was identified as a target in a subset of chromosomal translocations in non-Hodgkin lymphomas, leading to a juxtaposition of immunoglobulin 
-light chains to the FVT1-gene on chromosome 18, coupled with overexpression in certain T-cell malignancies. It is also located near the BCL-2 gene. Combined, these facts indicate involvement of FVT1 in tumourogenic processes (Rimokh et al 1993).
Another cytogenetic study identified WWOX, a human representative of the largest SDR cluster found in this study (cluster 8), as a gene product located on chromosome 16q23.3–24.1, a region affected frequently by allelic loss in breast cancer (Bednarek et al. 2000). Over-expression of WWOX in breast cancer compared to normal tissue was noted. Expression of this protein in other steroidogenic tissues such as prostate, ovary, and testis indicates that the intrinsic enzymatic WWOX activity is related to sex-steroid metabolism. This assumption is supported further by the tissue distribution and structural features of two other human forms found in this cluster, CGI-82 and PAN2. CGI-82 is expressed abundantly in the prostate and exhibits a low expression level in other tissues (Lin et al. 2001); PAN2 displays sequence similarities to other hydroxysteroid dehydrogenases.
Genome comparisons
Apart from the 8 SDR clusters present in all genomes investigated, orthologs to the human forms were detected in two model genomes for 11 SDR clusters and in one model genome for a further 10 SDR clusters (Table 2). The SDR forms missing in one or two of the model genomes probably have developed after the respective species divergence or have resulted from gene loss. Of all 31 clusters with SDR members in at least two genomes (Table 2), only two do not have a human representative.
Mammal-specific SDRs
We investigated the SDR enzymes present in only one of the genomes (Table 1). After reduction of close homologs within each species, each of the four genomes was found to have between 8 and 44 forms. The majority of these forms belong to the classical SDRs and have defined enzymatic functions such as steroid dehydrogenase or retinol dehydrogenase activities.
Sixteen forms were found in the human genome only, corresponding to 18 different proteins (Table 2, bottom). Homologs of all but three were found in other mammals, such as mouse, rat, cow, and pig. Close to half of these proteins are active on steroids, reflecting the importance of steroids in regulation of physiological functions and metabolic conversions in mammals. As deduced from their functions, these enzymes appear to be suitable targets for development of novel drugs directed at influencing hormone metabolism.
Clustering technique
The advantage of the clustering technique used in these genome comparisons, with the clusters formed by reciprocal relationships, is its insensitivity to the extent of residue identity or evolutionary speed. This is reflected by the fact that we could detect eight SDR clusters in all four genomes (Table 2), although intra-cluster residue conservation ranged from 46% to 7%. In some cases, the clustering procedure can be ambiguous; an example is cluster 8, which would otherwise separate into two clusters, one with the human WWOX form and one with the human PAN2 form, disregarding the A. thaliana forms. However, the A. thaliana members show mixed relationship with both sub-clusters; therefore, all forms are joined into one large cluster. As a consequence, orthologs to human forms of cluster 8 can be assigned only for D. melanogaster and C. elegans. The widespread nature of this cluster is also reflected by the fact that only a minor part (7%) of the multiple sequence alignment is strictly conserved (Table 2, cluster 8).
Evolutionary speed
The eight clusters with members from all four genomes were investigated with respect to their speed of divergence, after correction for multiple mutations according to Kimura (1983). The values obtained were divided with the value corresponding to the evolutionary divergence times for the animal–plant, worm–insect/mammal, and insect–mammal splits, reported to be 1215, 1045, and 850 million years, respectively (Feng et al. 1997). The clusters with extended SDRs were found to have evolutionary speeds of about 5 changes per 100 residues and 100 million years, whereas the clusters with classical SDRs have evolutionary speeds more than double this value. The slow evolution of the extended SDR enzymes is compatible with the conclusions drawn above that the extended SDR enzyme activities are present in most organisms and represent an ancient metabolic solution. However, the slow speed of the extended versus the classical SDRs is also compatible with the fact that most classical SDR subunits are smaller than the extended SDR subunits. Another case with two types of intrafamily evolutionary speed was noticed early on for the medium-chain dehydrogenase/reductase (MDR) alcohol dehydrogenases, in which "constant" and "variable" forms differ in speed from 6 to 18 changes per 100 residues and 100 million years (Jörnvall et al. 1993). Subsequently, that enzyme variability has been extended further to cover a >4-fold rate difference between slowly and rapidly evolving dehydrogenase species (Hjelmqvist et al. 1995).
SDR enzyme activities
The substrate spectrum of SDR enzymes with characterized activities is widespread (Table 2). Assuming a function in sugar and nucleotide metabolism for extended SDRs, we anticipate a related function for the ancestral SDR progenitor. Along with the appearance of steroid molecules, requiring the presence of oxygen, adaptation and development of classical SDRs with novel substrate specificities might have occurred. In line with this conclusion, it has been noted that bacterial steroid-metabolising enzymes are not only of the SDR type, but also of the cytochrome P450 type (CYP; Nelson 1999), indicating a role for cholesterol derivatives even in prokaryotes. Interestingly, CYP and SDR members do not appear only to complement each other in several distinct pathways of hormones and mediators (New and White 1995), or in xenobiotic metabolism, but they also display broad substrate specificities. Both superfamilies have numerous members in the genomes investigated thus far, indicating their importance for multi-cellular life. The families are of similar sizes, with 50–80 members in worm and mammals and >130 in A. thaliana. Several knockout models or genetic variants have proven the essential role of SDRs in development and homeostasis in humans (Geissler et al 1994; cf. Oppermann et al. 2001 and references therein), insects (Torroja et al. 1998), and plants (DeLong et al. 1993). Along with the determination of novel ligands for orphan receptors (Peet et al. 1998; Chawla et al. 2000), we assume that novel activities and functions for SDRs will be found (Nobel et al. 2001), a task for the next phase of functional genomics in SDR research.
|
Materials and methods |
|---|
|
TOPAbstractIntroductionResults and DiscussionMaterials and methodsReferences |
|---|
The members identified in the different genomes were clustered using a procedure similar to the one described for genome analysis (Tatusov et al. 1997). Automated ortholog servers exist, for example, TOGA (Quackenbush et al. 2000) and HomoloGene (Wheeler et al. 2001), clustering sequences at the nuclueotide level. In this paper, we focus on the SDR family and cluster the members at the protein level. FASTA3 was used to compare every member against the genome databases. Sequences were clustered according to these comparisons, defining a cluster as a group, in which every member ranks every other member higher than the first non-member. The cluster assignments are reciprocal, that is, usage of either sequence as the query sequence results in the proper sequence detection. These clusters will in most cases correspond to orthologs.
Evolutionary distances
Clusters with protein sequences from all four genomes were aligned using ClustalW (Thompson et al. 1994). The observed distances between the homologs in an alignment were calculated over comparable positions, (i.e., excluding gaps). These distances were then corrected for multiple hits according to Kimura (1983). The evolutionary distances between the homologs were calculated using the divergence times of Doolittle (Feng et al. 1997), 1215 Mya for the plant–animal separation, 1045 Mya for the worm–insect/mammal separation, and 850 Mya for the insect–mammal separation.
|
Acknowledgments |
|---|
The publication costs of this article were defrayed in part by payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 USC section 1734 solely to indicate this fact.
|
References |
|---|
|
TOPAbstractIntroductionResults and DiscussionMaterials and methodsReferences |
|---|
Bairoch, A. and Apweiler, R. 2000. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucleic Acids Res. 28:45–48.
Bancroft, I. 2000. Insights into the structural and functional evolution of plant genomes afforded by the nucleotide sequences of chromosomes 2 and 4 of Arabidopsis thaliana. Yeast 17:1–5.[CrossRef][Medline]
Bednarek, A.K., Laflin, K.J., Daniel, R.L., Liao, Q., Hawkins, K.A., and Aldaz, C.M. 2000. WWOX, a novel WW domain-containing protein mapping to human chromosome 16q23.3–24.1, a region frequently affected in breast cancer. Cancer Res. 60:2140–2145.
Chawla, A., Saez, E., and Evans, R.M. 2000. Don't know much bile-ology. Cell 103:1–4.[CrossRef][Medline]
DeLong A., Calderon-Urrea A., and Dellaporta S.L. 1993. Sex determination gene TASSELSEED2 of maize encodes a short-chain alcohol dehydrogenase required for stage-specific floral organ abortion. Cell 74:757–768.[CrossRef][Medline]
Feng, D.F., Cho, G., and Doolittle, R.F. 1997. Determining divergence times with a protein clock: Update and reevaluation. Proc. Natl Acad. Sci. 94:13028–13033.
Fransen, M., Van Veldhoven, P.P., and Subramani, S. 1999. Identification of peroxisomal proteins by using M13 phage protein VI phage display: Molecular evidence that mammalian peroxisomes contain a 2,4-dienoyl-CoA reductase. Biochem. J. 340:561–568.
Gabrielli, F., Donadel, G., Bensi, G., Heguy, A., and Melli, M. 1995. A nuclear protein, synthesized in growth-arrested human hepatoblastoma cells, is a novel member of the short-chain alcohol dehydrogenase family. Eur. J. Biochem. 232:473–477.[Medline]
Geissler, W.M., Davis, D.L., Wu, L., Bradshaw, K.D., Patel, S., Mendonca, B.B., Elliston, K.O., Wilson, J.D., Russell, D.W., and Andersson, S. 1994. Male pseudohermaphroditism caused by mutations of testicular 17 beta-hydroxysteroid dehydrogenase 3. Nat. Genet. 7:34–39.[CrossRef][Medline]
Ghosh, D., Sawicki, M., Pletnev, V., Erman, M., Ohno, S., Nakajin, S., and Duax, W.L. 2001. Porcine carbonyl reductase: Structural basis for a functional monomer in short chain dehydrogenases/reductases. J. Biol. Chem. 276:18457–18463.
Hjelmqvist, L., Estonius, M., and Jörnvall, H. 1995. The vertebrate alcohol dehydrogenase system: Variable class II type form elucidates separate stages of enzymogenesis. Proc. Natl Acad. Sci. 92:10905–10909.
Huala, E., Dickerman, A.W., Garcia-Hernandez, M., Weems, D., Reiser, L., LaFond, F., Hanley, D., Kiphart, D., Zhuang, M., Huang, W., Mueller, L.A., Bhattacharyya, D., Bhaya, D., Sobral, B.W., Beavis, W., Meinke, D.W., Town, C.D., Somerville, C., and Rhee, S.Y. 2001. The Arabidopsis Information Resource (TAIR): A comprehensive database and web-based information retrieval, analysis, and visualization system for a model plant. Nucleic Acids Res. 29:102–105.
International Human Genome Sequencing Consortium 2001. Initial sequencing and analysis of the human genome. Nature 409:860–921.[CrossRef][Medline]
Jörnvall, H., Persson, B., and Jörnvall, H. 1993. Variability patterns of dehydrogenases versus peptide hormones and proteases/antiproteases. FEBS Lett. 335:69–72.[CrossRef][Medline]
Jörnvall, H., Persson, B., Krook, M., Atrian, S., Gonzalez-Duarte, R., Jeffery, J., and Ghosh, D. 1995. Short-chain dehydrogenases/reductases (SDR). Biochemistry 34:6003–6013.[CrossRef][Medline]
Jörnvall, H., Höög, J.-O., and Persson, B. 1999. SDR and MDR: Completed genome sequences show these protein families to be large, of old origin, and of complex nature. FEBS Lett. 445:261–264.[CrossRef][Medline]
Kallberg, Y. and Persson, B. 1999. KIND — a nonredundant protein database. Bioinformatics 15:260–261.
Karplus, K., Barrett, C., and Hughey, R. 1998. Hidden Markov models for detecting remote protein homologies. Bioinformatics 14:846–856.
Kimura, M. 1983. The neutral theory of molecular evolution. Cambridge University Press, Cambridge, UK.
Krook, M., Ghosh, D., Strömberg, R., Carlquist, M., and Jörnvall, H. 1993. Carboxyethyllysine in a protein: Native carbonyl reductase/NADP+-dependent prostaglandin dehydrogenase. Proc. Natl Acad. Sci. 90:502–506.
Lin, B., White, J.T., Ferguson, C., Wang, S., Vessella, R., Bumgarner, R., True, L.D., Hood, L., and Nelson, P.S. 2001. Prostate short-chain dehydrogenase reductase 1 (PSDR1): A new member of the short-chain steroid dehydrogenase/reductase family highly expressed in normal and neoplastic prostate epithelium. Cancer Res. 61:1611–1618.
Nelson, D.R. 1999. Cytochrome P450 and the individuality of species. Arch. Biochem. Biophys. 369:1–10.[CrossRef][Medline]
New, M.I. and White, P.C. 1995. Genetic disorders of steroid hormone synthesis and metabolism. Baillieres Best Pract. Res. Clin. Endocrinol. Metab. 9:525–554.
Nobel, S., Abrahmsen, L., and Oppermann, U.H. 2001. Metabolic conversion as a pre-receptor control mechanism for lipophilic hormones. Eur. J. Biochem. 268:4113–4125.[Medline]
Oppermann, U.C., Persson, B., Filling, C., and Jörnvall, H. 1997. Structure–function relationships of SDR hydroxysteroid dehydrogenases. Adv. Exp. Med. Biol. 414:403–415.[Medline]
Oppermann, U.C., Filling, C., and Jörnvall, H. 2001. Forms and functions of human SDR enzymes. Chem. Biol. Interact. 130–132:699–705.
Pearson, W.R. and Lipman, D.J. 1988. Improved tools for biological sequence comparison. Proc. Natl Acad. Sci. 85:2444–2448.
Peet, D.J., Janowski, B.A., and Mangelsdorf, D.J. 1998. The LXRs: A new class of oxysterol receptors. Curr. Opin. Genet. Dev. 8:571–575.[CrossRef][Medline]
Persson, B., Krook, M., and Jörnvall, H. 1995. Short-chain dehydrogenases/reductases. Adv. Exp. Med. Biol. 372:383–395.[Medline]
Quackenbush, J., Liang, F., Holt, I., Pertea, G., and Upton, J. 2000. The TIGR gene indices: Reconstruction and representation of expressed gene sequences. Nucleic Acids Res. 28:141–145.
Rimokh, R., Gadoux, M., Bertheas, M.F., Berger, F., Garoscio, M., Deleage, G., Germain, D., and Magaud, J.P. 1993. FVT-1, a novel human transcription unit affected by variant translocation t(2;18)(p11;q21) of follicular lymphoma. Blood 81:136–142.
Russell, D.W. 2000. Oxysterol biosynthetic enzymes. Biochim. Biophys. Acta 1529:126–135.[Medline]
Tatusov, R.L., Koonin, E.V., and Lipman, D.J. 1997. A genomic perspective on protein families. Science 278:631–637.
Torroja, L., Ortuno-Sahagun, D., Ferrus, A., Hammerle, B., and Barbas, J.A. 1998. scully, an essential gene of Drosophila, is homologous to mammalian mitochondrial type II L-3-hydroxyacyl-CoA dehydrogenase/amyloid-ß peptide-binding protein. J. Cell Biol. 141:1009–1017.
Venter, J.C., Adams, M.D., Myers, E.W., Li, P.W., Mural, R.J., Sutton, G.G., Smith, H.O., Yandell, M., Evans, C.A., Holt, R.A., et al. 2001. The sequence of the human genome. Science 291:1304–1351.
Wheeler, D.L., Church, D.M., Lash, A.E., Leipe, D.D., Madden, T.L., Pontius, J.U., Schuler, G.D., Schriml, L.M., Tatusova, T.A., Wagner, L., and Rapp, B.A. 2001. Database resources of the National Center for Biotechnology Information. Nucleic Acids Res. 29:11–16.
Wilson, R.K. 1999. How the worm was won. The C. elegans genome sequencing project. Trends Genet. 15:51–58.[CrossRef][Medline]
CiteULike 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  A. Thorn, C. Egerer-Sieber, C. M. Jager, V. Herl, F. Muller-Uri, W. Kreis, and Y. A. Muller The Crystal Structure of Progesterone 5{beta}-Reductase from Digitalis lanata Defines a Novel Class of Short Chain Dehydrogenases/Reductases J. Biol. Chem., June 20, 2008; 283(25): 17260 - 17269. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. V. Entchev, D. Schwudke, V. Zagoriy, V. Matyash, A. Bogdanova, B. Habermann, L. Zhu, A. Shevchenko, and T. V. Kurzchalia LET-767 Is Required for the Production of Branched Chain and Long Chain Fatty Acids in Caenorhabditis elegans J. Biol. Chem., June 20, 2008; 283(25): 17550 - 17560. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 K. Vandenbroucke, S. Robbens, K. Vandepoele, D. Inze, Y. Van de Peer, and F. Van Breusegem Hydrogen Peroxide-Induced Gene Expression across Kingdoms: A Comparative Analysis Mol. Biol. Evol., March 1, 2008; 25(3): 507 - 516. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 O. A. B. S. M. Gani, O. A. Adekoya, L. Giurato, F. Spyrakis, P. Cozzini, S. Guccione, J.-O. Winberg, and I. Sylte Theoretical Calculations of the Catalytic Triad in Short-Chain Alcohol Dehydrogenases/Reductases Biophys. J., February 15, 2008; 94(4): 1412 - 1427. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. Fruscione, L. Sturla, G. Duncan, J. L. Van Etten, P. Valbuzzi, A. De Flora, E. Di Zanni, and M. Tonetti Differential Role of NADP+ and NADPH in the Activity and Structure of GDP-D-mannose 4,6-Dehydratase from Two Chlorella Viruses J. Biol. Chem., January 4, 2008; 283(1): 184 - 193. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 F. Li, T. Asami, X. Wu, E. W.T. Tsang, and A. J. Cutler A Putative Hydroxysteroid Dehydrogenase Involved in Regulating Plant Growth and Development Plant Physiology, September 1, 2007; 145(1): 87 - 97. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Rahier, S. Darnet, F. Bouvier, B. Camara, and M. Bard Molecular and Enzymatic Characterizations of Novel Bifunctional 3beta-Hydroxysteroid Dehydrogenases/C-4 Decarboxylases from Arabidopsis thaliana J. Biol. Chem., September 15, 2006; 281(37): 27264 - 27277. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
K. Guo, P. Lukacik, E. Papagrigoriou, M. Meier, W. H. Lee, J. Adamski, and U. Oppermann Characterization of Human DHRS6, an Orphan Short Chain Dehydrogenase/Reductase Enzyme: A NOVEL, CYTOSOLIC TYPE 2 R-beta-HYDROXYBUTYRATE DEHYDROGENASE J. Biol. Chem., April 14, 2006; 281(15): 10291 - 10297. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. H. Thomas Analysis of Homologous Gene Clusters in Caenorhabditis elegans Reveals Striking Regional Cluster Domains Genetics, January 1, 2006; 172(1): 127 - 143. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Kasus-Jacobi, J. Ou, D. G. Birch, K. G. Locke, J. M. Shelton, J. A. Richardson, A. J. Murphy, D. M. Valenzuela, G. D. Yancopoulos, and A. O. Edwards Functional Characterization of Mouse RDH11 as a Retinol Dehydrogenase Involved in Dark Adaptation in Vivo J. Biol. Chem., May 27, 2005; 280(21): 20413 - 20420. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
D. J. Hosfield, Y. Wu, R. J. Skene, M. Hilgers, A. Jennings, G. P. Snell, and K. Aertgeerts Conformational Flexibility in Crystal Structures of Human 11{beta}-Hydroxysteroid Dehydrogenase Type I Provide Insights into Glucocorticoid Interconversion and Enzyme Regulation J. Biol. Chem., February 11, 2005; 280(6): 4639 - 4648. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. Hormann, M. Kuchler, D. Sveshnikov, U. Oppermann, Y. Li, and J. Soll Tic32, an Essential Component in Chloroplast Biogenesis J. Biol. Chem., August 13, 2004; 279(33): 34756 - 34762. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. M. Torkko, K. T. Koivuranta, A. J. Kastaniotis, T. T. Airenne, T. Glumoff, M. Ilves, A. Hartig, A. Gurvitz, and J. K. Hiltunen Candida tropicalis Expresses Two Mitochondrial 2-Enoyl Thioester Reductases That Are Able to Form Both Homodimers and Heterodimers J. Biol. Chem., October 17, 2003; 278(42): 41213 - 41220. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. Kasus-Jacobi, J. Ou, Y. K. Bashmakov, J. M. Shelton, J. A. Richardson, J. L. Goldstein, and M. S. Brown Characterization of Mouse Short-chain Aldehyde Reductase (SCALD), an Enzyme Regulated by Sterol Regulatory Element-binding Proteins J. Biol. Chem., August 22, 2003; 278(34): 32380 - 32389. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
T. J. Bollenbach and D. B. Stern Secondary Structures Common to Chloroplast mRNA 3'-Untranslated Regions Direct Cleavage by CSP41, an Endoribonuclease Belonging to the Short Chain Dehydrogenase/Reductase Superfamily J. Biol. Chem., July 3, 2003; 278(28): 25832 - 25838. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Filling, K. D. Berndt, J. Benach, S. Knapp, T. Prozorovski, E. Nordling, R. Ladenstein, H. Jornvall, and U. Oppermann Critical Residues for Structure and Catalysis in Short-chain Dehydrogenases/Reductases J. Biol. Chem., July 5, 2002; 277(28): 25677 - 25684. [Abstract] [Full Text] [PDF]
|
|
| ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
