1. Lee Y, Jeon K, Lee JT, Kim S, Kim VN. MicroRNA maturation: stepwise processing and subcellular localization. Embo J. 2002;21(17):4663-4670 2. Chen K, Rajewsky N. The evolution of gene regulation by transcription factors and microRNAs. Nat Rev Genet. 2007;8(2):93-103 3. Pillai RS, Bhattacharyya SN, Filipowicz W. Repression of protein synthesis by miRNAs: how many mechanisms?. Trends Cell Biol. 2007;17(3):118-126 4. Walker GJ, Indsto JO, Sood R. et al. Deletion mapping suggests that the 1p22 melanoma susceptibility gene is a tumor suppressor localized to a 9-Mb interval. Genes Chromosomes Cancer. 2004;41(1):56-64 5. Bemis LT, Chen R, Amato CM. et al. MicroRNA-137 targets microphthalmia-associated transcription factor in melanoma cell lines. Cancer Res. 2008;68(5):1362-1368 6. Chinnadurai G. The transcriptional corepressor CtBP: a foe of multiple tumor suppressors. Cancer Res. 2009;69(3):731-734 7. Haflidadottir BS, Bergsteinsdottir K, Praetorius C, Steingrimsson E. miR-148 regulates Mitf in ...
Androgen-regulated short-chain dehydrogenase/reductase 1, ARSDR1CGI82, EC 1.1.1.300, HCBP12, HCV core-binding protein HCBP12, MDT1, prostate short-chain dehydrogenase reductase 1, Prostate short-chain dehydrogenase/reductase 1, PSDR1FLJ32633, RALR1, RalR1, Retinal reductase 1, retinol dehydrogenase 11, retinol dehydrogenase 11 (all-trans and 9-cis), retinol dehydrogenase 11 (all-trans/9-cis/11-cis), SCALD, SDR7C1, short chain dehydrogenase/reductase family 7C, member ...
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EC 1.1.1, EC 1.1.1.-, FLJ16333, MGC126600, Orphan short-chain dehydrogenase/reductase, RDH-S, RDHSMGC126602, SDR-Oorphan short-chain dehydrogenase / reductase, SDROretinol dehydrogenase similar protein, short-chain dehydrogenase/reductase family 9C member 7, short chain dehydrogenase/reductase family 9C, member ...
Estradiol 17-beta-dehydrogenase 11,1.1.1.62,17-beta-hydroxysteroid dehydrogenase 11,17-beta-HSD 11,17bHSD11,17betaHSD11,17-beta-hydroxysteroid dehydrogenase XI,17-beta-HSD XI,17betaHSDXI,Cutaneous T-cell lymphoma-associated antigen HD-CL-03,CTCL-associated antigen HD-CL-03,Dehydrogenase/reductase SDR family member 8,Retinal short-chain dehydrogenase/reductase 2,retSDR2,Short chain dehydrogenase/reductase family 16C member 2,HSD17B11,DHRS8,PAN1B,SDR16C2,PSEC0029,UNQ207/PRO233,. ...
Corepressor targeting diverse transcription regulators such as GLIS2 or BCL6. Has dehydrogenase activity. Involved in controlling the equilibrium between tubular and stacked structures in the Golgi complex. Functions in brown adipose tissue (BAT) differentiation.
BACKGROUND: (R)-[3,5-bis(trifluoromethyl)phenyl] ethanol [(R)-3,5-BTPE] is a valuable chiral intermediate for Aprepitant (Emend) and Fosaprepitant (Ivemend). Biocatalyzed asymmetric reduction is a preferred approach to synthesize highly optically active (R)-3,5-BTPE. However, the product concentration and productivity of reported (R)-3,5-BTPE synthetic processes remain unsatisfied. RESULTS: A NADPH-dependent carbonyl reductase from Lactobacillus kefir (LkCR) was discovered by genome mining for reduction of 3,5-bis(trifluoromethyl) acetophenone (3,5-BTAP) into (R)-3,5-BTPE with excellent enantioselectivity. In order to synthesize (R)-3,5-BTPE efficiently, LkCR was coexpressed with glucose dehydrogenase from Bacillus subtilis (BsGDH) for NADPH regeneration in Escherichia coli BL21 (DE3) cells, and the optimal recombinant strain produced 250.3 g/L (R)-3,5-BTPE with 99.9% ee but an unsatisfied productivity of 5.21 g/(L h). Then, four different linker peptides were used for the fusion expression of ...
The major metabolic pathways involved in synthesis and disposition of carbonyl and hydroxyl group containing compounds are presented, and structural and functional characteristics of the enzyme families involved are discussed. Alcohol and aldehyde dehydrogenases (ADH, ALDH) participate in oxidative pathways, whereas reductive routes are accomplished by members of the aldo-keto reductase (AKR), short-chain dehydrogenases/reductases (SDR) and quinone reductase (QR) superfamilies. A wealth of biochemical, genetic and structural data now establishes these families to constitute important phase I enzymes.
Complete information for SDR42E1 gene (Protein Coding), Short Chain Dehydrogenase/Reductase Family 42E, Member 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Dehydrogenase/reductase (SDR family) member 7 (DHRS7, retSDR4, SDR34C1) is a previously uncharacterized member of the short-chain dehydrogenase/reductase (SDR) superfamily. While human SDR members are known to play an important role in various (patho)biochemical pathways including intermediary metabolism and biotransformation of xenobiotics, only 20% of them are considered to be well characterized. Based on phylogenetic tree and SDR sequence clusters analysis DHRS7 is a close relative to well-known SDR member 11β-hydroxysteroid dehydrogenase 1 (11β-HSD1) that participates in metabolism of endogenous and xenobiotic substances with carbonyl group. The aim of present study is to determine the basic biochemical properties of DHRS7 and its possible involvement in metabolism of substrates with carbonyl group. For the first time the computational predictions of this membrane protein and membrane topology were experimentally confirmed. DHRS7 has been demonstrated to be an integral protein facing the lumen of
retinol dehydrogenase 8 (all trans) Proteins available through Novus Biologicals. Browse our retinol dehydrogenase 8 (all trans) Protein catalog backed by our Guarantee+.
592 Drug resistance caused by overexpression of P-glycoprotein (P-gp), the MDR1 gene product, limits the therapeutic outcome in cancer patients. Although modulation of multidrug resistance (MDR) by pharmacological agents, antibodies, antisense oligonucleotides, siRNA, and inhibitors of signal transduction have been reported, clinical benefits have been disappointing. We and others have sought to understand the regulation of MDR1 gene expression as another approach to this problem. CtBP1 (C-terminal-binding protein 1) is a transcriptional co-regulator that plays an important role in oncogenesis. Recently, it was reported that CtBP1 could serve as both a co-activator and co-repressor of transcription. In this study, we determined the effect of CtBP1 on transcription of the MDR1 gene. Chromatin immunoprecipitation (ChIP) experiments demonstrated that CtBP1 bound to the promoter and coding regions of the MDR1 gene, but not to the non-coding regions. Knockdown of CtBP1 expression by siRNA repressed ...
Alcohol Oxidase, 10 mg. Alcohol Oxidase (AOX) is a homooctameric flavoprotein consisting of eight identical subunits of ~74 kD, each containing a flavin adenine dinucleotide molecule (FAD) as a prosthetic group (van der Klei et al.
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
Shop Dehydrogenase/reductase SDR family protein ELISA Kit, Recombinant Protein and Dehydrogenase/reductase SDR family protein Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
CP000667.PE408 Location/Qualifiers FT CDS_pept 469214..469912 FT /codon_start=1 FT /transl_table=11 FT /locus_tag="Strop_0408" FT /product="short-chain dehydrogenase/reductase SDR" FT /note="PFAM: short-chain dehydrogenase/reductase SDR" FT /db_xref="EnsemblGenomes-Gn:Strop_0408" FT /db_xref="EnsemblGenomes-Tr:ABP52893" FT /db_xref="InterPro:IPR002347" FT /db_xref="InterPro:IPR036291" FT /db_xref="UniProtKB/TrEMBL:A4X1Z3" FT /protein_id="ABP52893.1" FT /translation="MVNLDGLRVAVTGAGRASGRLLATAFAEHGAQVFVSARDEVAARR FT TTDSIRQRGRGRGEAFVCDLTSPDSVRAFAAALTDRTDHLDVLVNNGAGYLHGVDLGDV FT EDDHIIATIGGTATGTVLLTKHLLALLRASTRPDIVNMISACGEVGHHRSEAHPAFYAA FT KHAQAGFAEIMSHRLRVEGIRVISLFPPDFVQHGPRVASNNLTAQSVVDCVLFAVSQPR FT DCFIREFRFE" gtggtgaatc tcgacggact acgggttgct gtcaccggcg ccgggcgcgc ctccggacgc 60 ctcctggcga ccgccttcgc cgagcacggc gcgcaggtgt ttgtctccgc ccgtgatgag 120 gtggcagcca gacgcaccac ggattcgatc cggcagcgtg ggcgggggag aggcgaagcc 180 ttcgtctgtg acctgaccag ccccgactcg gtacgcgcgt tcgcggcggc gttgaccgac 240 cgcaccgacc ...
But experimentalists should not get too cocky: the next paper, by Jamie Simpson and collaborators at Monash University, describes some of the things that can go wrong. An STD NMR screen of the antimicrobial target ketopantoate reductase (KPR) using the same Maybridge library of 500 compounds revealed 196 hits! The 47 with the strongest STD signals were then tested in a 1H/15N-HSQC NMR assay, leading to 14 hits, of which 4 gave measurable IC50 values in an enzymatic assay. Unfortunately, follow-up SAR was disappointing, and subsequent experiments revealed that aggregation was to blame: when the biochemical experiments were rerun in the presence of 0.01% Tween-20, only a single fragment gave a measurable IC50 value. The researchers redid their STD-NMR screen in the presence of detergent, resulting in 71 hits, all of which were tested in the biochemical screen. This led to the identification of a new (and fairly potent) hit that had previously been missed. This nicely illustrates the fact that ...
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Complete information for RDH16 gene (Protein Coding), Retinol Dehydrogenase 16 (All-Trans), including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
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RDH5兔多克隆抗体(ab101457)可与人样本反应并经WB, IHC实验严格验证。中国75%以上现货,所有产品均提供质保服务,可通过电话、电邮或微信获得本地专属技术支持。
TY - JOUR. T1 - Cloning and sequence analysis of a cDNA for 3-hydroxyisobutyrate dehydrogenase. Evidence for its evolutionary relationship to other pyridine nucleotide-dependent dehydrogenases. AU - Rougraff, P. M.. AU - Zhang, B.. AU - Kuntz, M. J.. AU - Harris, Robert. AU - Crabb, David. PY - 1989. Y1 - 1989. N2 - A 1.7-kilobase pair cDNA clone encoding 3-hydroxyisobutyrate dehydrogenase has been isolated by screening a rat liver λgt11 library with a 17-base oligonucleotide probe which corresponds to a portion of the N-terminal amino acid sequence of rabbit liver 3-hydroxyisobutyrate dehydrogenase. The cDNA contains an open reading frame of 1038 base pairs which includes an amino acid sequence that matches the N-terminal 35 amino acid sequence of rabbit 3-hydroxyisobutyrate dehydrogenase at 33 residues. The cDNA predicts a 300-amino acid mature protein with an amino acid composition and molecular weight very similar to that of rabbit liver 3-hydroxyisobutyrate dehydrogenase. Northern blot ...
Looking for online definition of retinal reductase in the Medical Dictionary? retinal reductase explanation free. What is retinal reductase? Meaning of retinal reductase medical term. What does retinal reductase mean?
Définitions de 1 3 propanediol dehydrogenase, synonymes, antonymes, dérivés de 1 3 propanediol dehydrogenase, dictionnaire analogique de 1 3 propanediol dehydrogenase (anglais)
cinnamyl alcohol dehydrogenase: NADP-dependent enzyme that catalyzes the reversible conversion of p-hydroxycinnamaldehydes to their corresponding alcohols, leading to the biosynthesis of lignin in plants
This gene encodes a mitochondrial 3-hydroxyisobutyrate dehydrogenase enzyme. The encoded protein plays a critical role in the catabolism of L-valine by catalyzing the oxidation of 3-hydroxyisobutyrate to methylmalonate semialdehyde. [provided by RefSeq, Nov 2011 ...
Enzyme with hydroxy-pyruvate reductase, glyoxylate reductase and D-glycerate dehydrogenase enzymatic activities. Reduces hydroxypyruvate to D-glycerate, glyoxylate to glycolate oxidizes D-glycerate to hydroxypyruvate.
The corepressor CtBP (carboxyl-terminal binding protein) is involved in transcriptional pathways important for development, cell cycle regulation, and transformation. We demonstrate that CtBP binding to cellular and viral transcriptional repressors is regulated by the nicotinamide adenine dinucleotides NAD+ and NADH, with NADH being two to three orders of magnitude more effective. Levels of free nuclear nicotinamide adenine dinucleotides, determined using two-photon microscopy, correspond to the levels required for half-maximal CtBP binding and are considerably lower than those previously reported. Agents capable of increasing NADH levels stimulate CtBP binding to its partners in vivo and potentiate CtBP-mediated repression. We propose that this ability to detect changes in nuclear NAD+/NADH ratio allows CtBP to serve as a redox sensor for transcription. ...
CBR1_HUMAN RecName: Full=Carbonyl reductase [NADPH] 1; AltName: Full=15-hydroxyprostaglandin dehydrogenase [NADP(+)]; AltName: Full=NADPH-dependent carbonyl reductase 1; AltName: Full=Prostaglandin 9-ketoreductase; AltName: Full=Prostaglandin-E(2) 9-reductase ...
Nicotiana tabacum cDNA encoding a bifunctional protein having catalytic domains for dehydroquinase and shikimate dehydrogenase was cloned and sequenced. Complementation of Escherichia coli aroD and aroE auxotrophs was successful. Amino acid sequencing located the N-terminus of the mature protein. The two catalytic domains exhibited greater amino acid identity with prokaryote homologues than with yeast and fungal homologues. ...
Oksidoreduktase alkohol:NAD+ (bahasa Inggris: aldehyde reductase; alcohol dehydrogenase (NAD); aliphatic alcohol dehydrogenase; ethanol dehydrogenase; NAD-dependent alcohol dehydrogenase; NAD-specific aromatic alcohol dehydrogenase; NADH-alcohol dehydrogenase; NADH-aldehyde dehydrogenase; primary alcohol dehydrogenase; yeast alcohol dehydrogenase, NAD+ oxidoreductase, ADH; EC 1.1.1.1) adalah keluarga enzim dari golongan dehidrogenase yang berfungsi sebagai katalisator oksidasi alkohol dengan aldehid atau keton, dengan reduksi NAD+ menjadi NADH. ADH merupakan protein yang mengandung Zn yang bereaksi pada alkohol primer dan sekunder atau asetal-hemi, dan alkohol sekunder siklik.[1] Reaksi yang terjadi: ...
Thus, the two substrates of this enzyme are (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate and NAD+, whereas its 4 products are 2-oxoadipate, CO2, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate:NAD+ oxidoreductase (decarboxylating). Other names in common use include 2-hydroxy-3-carboxyadipate dehydrogenase, 3-carboxy-2-hydroxyadipate dehydrogenase, homoisocitric dehydrogenase, (−)-1-hydroxy-1,2,4-butanetricarboxylate:NAD+ oxidoreductase, (decarboxylating), 3-carboxy-2-hydroxyadipate:NAD+ oxidoreductase (decarboxylating), and HICDH. This enzyme participates in lysine biosynthesis. ...
Purchase Recombinant Escherichia coli Glyoxylate/hydroxypyruvate reductase A(ghrA). It is produced in Yeast. High purity. Good price.
Pseudomonas aeruginosa ExaE protein: a response regulator of a two-component regulatory system for controling expression quinoprotein ethanol dehydrogenase; isolated from Pseudomonas aeruginosa; amino acid sequence in first source
Accepted name: alcohol dehydrogenase (nicotinoprotein). Reaction: ethanol + acceptor - acetaldehyde + reduced acceptor. Other name(s): nicotinoprotein alcohol dehydrogenase; np-ADH; NDMA-dependent alcohol dehydrogenase; ethanol:N,N-dimethyl-4-nitrosoaniline oxidoreductase. Systematic name: ethanol:acceptor oxidoreductase. Comments: Contains Zn2+. Nicotinoprotein alcohol dehydrogenases are unique medium-chain dehydrogenases/reductases (MDR) alcohol dehydrogenases that have a tightly bound NAD+/NADH cofactor that does not dissociate during the catalytic process. Instead, the cofactor is regenerated by a second substrate or electron carrier. While the in vivo electron acceptor is not known, N,N-dimethyl-4-nitrosoaniline (NDMA), which is reduced to 4-(hydroxylamino)-N,N-dimethylaniline, can serve this function in vitro. The enzyme from the Gram-positive bacterium Amycolatopsis methanolica can accept many primary alcohols as substrates, including benzylalcohol [1].. Links to other databases: BRENDA, ...
Accepted name: coniferyl-alcohol dehydrogenase. Reaction: coniferyl alcohol + NADP+ = coniferyl aldehyde + NADPH + H+. Other name(s): CAD. Systematic name: coniferyl-alcohol:NADP+ oxidoreductase. Comments: Specific for coniferyl alcohol; does not act on cinnamyl alcohol, 4-coumaryl alcohol or sinapyl alcohol.. Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, CAS registry number: 37250-27-4. References:. 1. Mansell, R.L., Babbel, G.R. and Zenk, M.H. Multiple forms and specificity of coniferyl alcohol dehydrogenase from cambial regions of higher plants. Phytochemistry 15 (1976) 1849-1853.. 2. Wyrambik, D. and Grisebach, H. Purification and properties of isoenzymes of cinnamyl-alcohol dehydrogenase from soybean-cell-suspension cultures. Eur. J. Biochem. 59 (1975) 9-15. [PMID: 1250]. ...
1MGO: Mobility of Fluorobenzyl Alcohols Bound to Liver Alcohol Dehydrogenases as Determined by NMR and X-ray Crystallographic Studies
RDH10 is a specific all-trans retinol dehydrogenase identified in the RPE and now in the Müller cells. 14 We propose that one of the possible physiological functions of RDH10 is to synthesize the all-trans retinal chromophore for RGR and thus to act as a functional partner of RGR in the photic visual cycle. As RGR is known to be expressed in both the RPE and Müller cells, it was necessary to determine whether RDH10 co-expresses with RGR in both the RPE and Müller cells. Western blot analysis demonstrated that RDH10 is expressed at a high level in the RPE and a lower level in the retina (Fig. 2) . The anti-RDH10 antibody stained a cell type in the inner retina. The morphology of the stained cells and their location in the retina are consistent with those of Müller cells. 16 To further confirm the observation, we used rMC-1 cells, a well-established and characterized retinal Müller cell line. 19 RDH10 expression in this cell line was detected at both the mRNA and protein levels (Fig. 4) ...
Reitman and colleagues had a hunch that the genetic mutation seen in cancer might trigger a similar functional change to a closely related enzyme found in yeast and bacteria (homoisocitrate dehydrogenase), which would create the elusive 2-hydroxyadipate dehydrogenase necessary for "green" adipic acid production.. They were right. The functional mutation observed in cancer could be constructively applied to other closely related enzymes, creating a beneficial outcome - in this case the missing link that could enable adipic acid production from cheap sugars. The next step will be to scale up the overall adipic acid production process, which remains a considerable undertaking.. "Its exciting that sequencing cancer genomes can help us to discover new enzyme activities," Reitman said. "Even genetic changes that occur in only a few patients could reveal useful new enzyme functions that were not obvious before.". Yan, a professor in the Department of Pathology and senior author of the study, said the ...
TY - JOUR. T1 - Regulation of the expression of the rat alcohol dehydrogenase gene by glucocorticoids.. AU - Qulali, M.. AU - Wolfla, C. E.. AU - Ross, R. A.. AU - Crabb, D. W.. PY - 1989. Y1 - 1989. UR - http://www.scopus.com/inward/record.url?scp=0024491855&partnerID=8YFLogxK. UR - http://www.scopus.com/inward/citedby.url?scp=0024491855&partnerID=8YFLogxK. M3 - Article. C2 - 2471210. AN - SCOPUS:0024491855. VL - 290. SP - 143. EP - 153. JO - Progress in Clinical and Biological Research. JF - Progress in Clinical and Biological Research. SN - 0361-7742. ER - ...
negative regulation of all-trans-retinyl-ester hydrolase, 11-cis retinol forming activity - Ontology Report - Rat Genome Database
GT:ID BAD57618.1 GT:GENE BAD57618.1 GT:PRODUCT putative short chain dehydrogenase GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 2940013..2940783 GB:FROM 2940013 GB:TO 2940783 GB:DIRECTION + GB:PRODUCT putative short chain dehydrogenase GB:PROTEIN_ID BAD57618.1 LENGTH 256 SQ:AASEQ MDKDSFRKLFDLSGRTAIVTGGTRGIGLAIAEGFACAGANLVVASRKPEACEQAAARLRELGAQAVGVPTHLGEIDSLRALVDTAVSAFGGIDIVVNNAANALAQPLATMAPEAVDKSFGVNVQGPLFLVQAALPHLRASAHAAVLNLGSVAALQFAPGLSMYAAGKAALLSFTRAMAAEFAADGIRVNAMAPGAVNTDMVRKNPPEFIAAMAQAPLLRRIAEPDEMVGAALLLCSDAGSFITGQTFLVDGGTVAR GT:EXON 1,1-256:0, BL:SWS:NREP 1 BL:SWS:REP 12-,256,DHRS4_RABIT,4e-36,36.8,242/260, PROS 150-,178,PS00061,ADH_SHORT,PDOC00060, SEG 97-,102,nnaana, BL:PDB:NREP 1 BL:PDB:REP 9-,255,1vl8B,1e-34,34.4,247/252, RP:PDB:NREP 1 RP:PDB:REP 10-,256,2ae1A,8e-44,30.6,245/252, RP:PFM:NREP 1 RP:PFM:REP 15-,180,PF00106,2e-21,42.2,166/169,adh_short, HM:PFM:NREP 1 HM:PFM:REP 16-,181,PF00106,2.2e-34,30.9,162/167,adh_short, GO:PFM:NREP 2 GO:PFM ...
GT:ID BAD55466.1 GT:GENE BAD55466.1 GT:PRODUCT putative short chain dehydrogenase GT:DATABASE GIB00210CH01 GT:ORG nfar0 GB:ACCESSION GIB00210CH01 GB:LOCATION 643418..644293 GB:FROM 643418 GB:TO 644293 GB:DIRECTION + GB:PRODUCT putative short chain dehydrogenase GB:PROTEIN_ID BAD55466.1 LENGTH 291 SQ:AASEQ MSRWDTANIPDQSGRTFIVTGANSGLGAVAARALARAGADVVLACRNLTKAEKVAAEIGARATVRELDLADLASVRAFAAGTERVDVLINNAGVMAVPHRTTADGFEMQIGTNHLGHFALTGLLLDKITDRVVTVSSGAHAVGRIDLADLNWERRRYQRWLAYGQSKLANLLFAYELQRRLGAAGSPILSVAAHPGYAATELQSHTETFLDSVMNVGNRILAQTAEMGALPELFAATMPVEPGAFYGPTGLGGMRGYPGRCGSTKASRDERVAGELWALSERLTGVTYSFD GT:EXON 1,1-291:0, BL:SWS:NREP 1 BL:SWS:REP 7-,286,RDH13_MOUSE,2e-38,40.5,269/334, SEG 25-,44,glgavaaralaragadvvla, BL:PDB:NREP 1 BL:PDB:REP 14-,205,2japC,4e-08,39.4,180/246, RP:PDB:NREP 2 RP:PDB:REP 13-,91,2ag5C,1e-05,23.4,77/244, RP:PDB:REP 68-,205,3ce6B,5e-13,8.1,136/485, RP:PFM:NREP 1 RP:PFM:REP 46-,143,PF00106,3e-05,38.8,98/169,adh_short, HM:PFM:NREP 1 HM:PFM:REP ...
Contains NADP+ as a cofactor. This is the first enzyme in the biosynthetic pathway of pseudaminic acid [3], a sialic-acid-like sugar that is unique to bacteria and is used by Helicobacter pylori to modify its flagellin. This enzyme plays a critical role in H. pyloris pathogenesis, being involved in the synthesis of both functional flagella and lipopolysaccharides [1,2]. It is completely inhibited by UDP-alpha-D-galactose. The reaction results in the chirality of the C-5 atom being inverted. It is thought that Lys-133 acts sequentially as a catalytic acid, protonating the C-6 hydroxy group and as a catalytic base, abstracting the C-5 proton, resulting in the elimination of water. This enzyme belongs to the short-chain dehydrogenase/reductase family of enzymes ...
At concentrations of 2mM and above hydroxypyruvate produced no glucose with isolated rat liver cells, although it was rapidly utilized. At a lower concentration of hydroxypyruvate or in the presence of substrates which generate reducing equivalents (ethanol or butyrate), appreciable amounts of glucose were formed from hydroxypyruvate. A possible explanation for this phenomenon is discussed.. ...
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ADH4, class II alcohol dehydrogenase 4 pi subunit, which is a member of the alcohol dehydrogenase family. Members of this enzyme family metabolize a…
putative quinate/shikimate dehydrogenase [putative shikimate 5-dehydrogenase] ATGGTCAAGGACTCGTATCTCGTCGGGCTGATCGGCGCCGGGATCGGCCCGTCGCTCAGC CCGGCACTGCACGAGCGGGAGGCCGACCGGCAGGGCCTGCGCTATCTGTACCGGCTGATC GACATCGACGCGCTCGGTGTCGGGCCGCAGGCGGTGGGGGACCTCGTACGAGCCGCCCGC GACCTGGGCTTCGACGGGCTGAACATCACGCATCCCTGCAAGCAGCTCGTCATCGGGCAT CTGGACGCGCTCGCCCCGCAGGCCGAGGCGCTCGGCGCGGTGAACACCGTCGTCTTCGAG GGCGGGCGTGCGGTCGGGCACAACACCGATGTCACCGGGTTCGCCGCCTCGTTCGCCCGT GGGCTGCCGGATGCCCCGCTGGAGCGGGTCGTGCAGTTGGGCGCGGGGGGAGCGGGGGCG GCCGTCGCGCATGCCATGCTCACGCTCGGGGCCGGGCACGTCACCGTCGTCGATGCCATG CCGGACCGGTCGGCGGACCTCGCCGCCTCGCTGAACCGGCACTTCGGTGCGGGGCGGGCC GCTGCCGCGGGCCCGGAGCGGCTGGCGGCGCTGCTCGGCGGTGCGGACGGCATCGTGCAT GCCACGCCGACGGGGATGGCCGCTCATCCGGGGCTGCCGCTTCCCGGTGAGTTGCTGCAT CCCGGGTTGTGGGTGGCCGAGGTGGTGTACCGGCCGTTGGAGACCGAGTTGCTGCGTGCC GCTCGGGCGGCGGGGTGTGCGGTTCTCGATGGTGGGGGGATGGCTGTTTTCCAGGCCGCG GACGCGTTTCGGCTGTTCACGGGGCGGGAGCCGGACGCGGTGCGGATGCTTGCGGATATT ...
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NADP_Rossmann (CL0063) 2-Hacid_dh_C; D-isomer specific 2-hydroxyacid dehydrogenase, NAD binding domain (PF02826; HMM-score: 173.2) ...