1PII: Three-dimensional structure of the bifunctional enzyme phosphoribosylanthranilate isomerase: indoleglycerolphosphate synthase from Escherichia coli refined at 2.0 A resolution.
Background. The GNPDA2 (glucosamine-6-phosphate deaminase 2) gene is a member of Glucosamine-6-phosphate (GlcN6P) deaminase subfamily, which encoded an allosteric enzyme of GlcN6P. Genome-wide association studies (GWAS) have shown that variations of human GNPDA2 are associated with body mass index and obesity risk, but its function and metabolic implications remain to be elucidated.The object of this study was to characterize the gene structure, expression, and biological functions of GNPDA2 in chickens. Methods. Variant transcripts of chicken GNPDA2 and their expression were investigated using rapid amplification of cDNA ends (RACE) system and real-time quantitative PCR technology. We detected the GNPDA2 expression in hypothalamic, adipose, and liver tissue of Xinghua chickens with fasting and high-glucose-fat diet treatments, and performed association analysis of variations of GNPDA2 with productive traits in chicken. The function of GNPDA2 was further studied by overexpression and small interfering
In order to overproduce D-xylose isomerase, the Escherichia coli D-xylose isomerase (D-xylose ketol-isomerase, EC 5.3.1.5) gene (xylA) was fused to ${\lambda}P_{L}$ promoter. The promoterless xylA gene containing the ribosome binding site and coding region for D-xylose isomerase was cloned into a ...
In enzymology, a xylose isomerase (EC 5.3.1.5) is an enzyme that catalyzes the interconversion of D-xylose and D-xylulose. This enzyme belongs to the family of isomerases, specifically those intramolecular oxidoreductases interconverting aldoses and ketoses. The isomerase has now been observed in nearly a hundred species of bacteria. Xylose-isomerases are also commonly called fructose-isomerases due to their ability to interconvert glucose and fructose. The systematic name of this enzyme class is D-xylose aldose-ketose-isomerase. Other names in common use include D-xylose isomerase, D-xylose ketoisomerase, and D-xylose ketol-isomerase. The activity of D-xylose isomerase was first observed by Mitsuhashi and Lampen in 1953 in the bacterium Lactobacillus pentosus. Artificial production through transformed E.coli have also been successful. In 1957, the D-xylose isomerase activity on D-glucose conversion to D-fructose was noted by Kooi and Marshall. It is now known that isomerases have broad ...
casSAR Dugability of P25170 | TRPC | Multifunctional tryptophan biosynthesis protein - Also known as TRPG_PHACH, TRPC. Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities.
anthranilate synthase / indole-3-glycerol phosphate synthase / phosphoribosylanthranilate isomerase [EC:4.1.3.27 4.1.1.48 5.3.1.24 ...
Keywords: Keywords: DNA methylation - Gene silencing - RNA-directed DNA methylation - RNA interference - Transposon.; Abbreviations: Ac, Activator; BAL, BALL; CMT, CHROMOMETHYLASE; DDM, DECREASE IN DNA METHYLATION; DRM, DOMAIN REARRANGED METHYLTRANSFERASE; En/Spm, Enhancer/Suppressor-mutator; MET, METHYLTRANSFERASE; MOP, MODIFIER OF PARAMUTATION; PAI, PHOSPHORIBOSYLANTHRANILATE ISOMERASE; PTGS, post-transcriptional gene silencing; RdDM, RNA-directed DNA methylation; RNAi, RNA interference; SUP, SUPERMAN; TGS, transcriptional gene silencing; TSI, transcriptionally silent information. Journal Article. 5263 words. Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry ...
1K5H: Crystal structure of 1-deoxy-D-xylulose-5-phosphate reductoisomerase, a crucial enzyme in the non-mevalonate pathway of isoprenoid biosynthesis.
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
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Perform reliable qPCR with Bio-Rads pre-validated GNPDA2 primer pair, for the Chicken genome. Designed for SYBR Green-based detection.
GNPDA1 Antibody 12312-1-AP has been identified with IHC, WB, ELISA. 12312-1-AP detected 33 kDa band in K-562 cells with 1:500-1:2000 dilution...
GNPDA2 Antibody 17105-1-AP has been identified with IHC, WB, ELISA. 17105-1-AP detected 31 kDa band in rat kidney tissue with 1:500-1:1000 dilution...
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Note from Pfam: this protein didnt match Pfam, but it pretty soon became clear that this protein should have belonged to PF01182. I have rebuilt that family to include this protein. Gene YP_001050605 from SHEWANELLA BALTICA OS155 encodes a protein with 232 residues, whcih has annotated 6-phosphogluconolactonase. Sequence alignment indicates that this proteim belongs to the sugarP_isomerase superfamily. Dali search even suggests this target be a glucose-6-phosphate 1-dehydrogenase or glucosamine-6-phosphate deaminase. More details for this structures investigation will be presented in the future hopefully. ...
MetabolismCentral intermediary metabolismAmino sugarsglucosamine-6-phosphate deaminase (TIGR00502; EC 3.5.99.6; HMM-score: 33.2) ...
D-xylose isomerase (XI) is capable of sugar isomerization and slow conversion of some monosaccharides into their C2-epimers. We present X-ray and neutron ...
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MetabolismBiosynthesis of cofactors, prosthetic groups, and carriersOther1-deoxy-D-xylulose-5-phosphate synthase (TIGR00204; EC 2.2.1.7; HMM-score: 20.4) ...
Isomerases are a broad class of enzymes which catalyze structural change in a single molecule in biological systems. These structural changes can be ext...
Phosphoribosylanthranilate isomerase and indoleglycerol-phosphate synthase: tryptophan biosynthetic enzymes from Thermotoga maritima ...
292123913 - EP 1095153 A1 2001-05-02 - BIOLOGICAL TAGATOSE PRODUCTION BY RECOMBINANT ESCHERICHIA COLI - [origin: WO0068397A1] This invention relates to a recombinant i Escherichia coli /i and a process for producing D-tagatose. In detail, it includes the construction of recombinant i E.coli /i harboring L-arabinose isomerase, whole-cell conversion of D-galactose into D-tagatose by recombinant i E.coli /i expressing L-arabinose isomerase, enzymatic production of D-tagatose by the extract of recombinant i E.coli /i expressing L-arabinose isomerase, and bioconversion by immobilized L-arabinose isomerase.[origin: WO0068397A1] This invention relates to a recombinant i Escherichia coli /i and a process for producing D-tagatose. In detail, it includes the construction of recombinant i E.coli /i harboring L-arabinose isomerase, whole-cell conversion of D-galactose into D-tagatose by recombinant i E.coli /i expressing L-arabinose isomerase, enzymatic production of D-tagatose by the extract of
Background L-arabinose isomerase (AI) is a crucial catalyst for the biotransformation of D-galactose to D-tagatose. In previous reports, AIs from thermophilic bacterial strains had been wildly...
p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.,/p> ,p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.,/p> ,p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).,/p> ,p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x,sup>64,/sup> + x,sup>4,/sup> + x,sup>3,/sup> + x + 1. The algorithm is described in the ISO 3309 standard. ,/p> ,p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.,br /> ,strong>Cyclic redundancy and other checksums,/strong>,br /> ,a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993),/a>),/p> Checksum:i ...
Tuberculosis, caused by the pathogenic bacteria Mycobacterium tuberculosis, is one of the most widespread and deadly infectious diseases today. Treatment of tuberculosis relies on antibiotics that were developed more than 50 years ago. These are now becoming ineffective due to the emergence of antibiotic resistant strains of the bacteria.. The aim of the research in this thesis was to develop new antibiotics for tuberculosis treatment. To this end, we targeted enzymes from two essential biosynthetic pathways in M. tuberculosis for drug development. The methylerythritol phosphate (MEP) pathway synthesizes a group of compounds called isoprenoids. These compounds have essential roles in all living organisms. The fact that humans utilize a different pathway for isoprenoid synthesis makes the MEP pathway enzymes attractive targets for drug development. We have determined the structures of two essential enzymes from this pathway by X-ray crystallography: 1-deoxy-D-xylulose 5-phosphate reductoisomerase ...
SWISS-MODEL Repository entry for C4L656 (DXR_EXISA), 1-deoxy-D-xylulose 5-phosphate reductoisomerase. Exiguobacterium sp (strain ATCC BAA-1283 / AT1b)
Glucose-6-phosphate isomerase (GPI) (EC 5.3.1.9) or phosphoglucose isomerase (PGI) [1,2] is a dimeric enzyme that catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. PGI is involved in different pathways: in most higher organisms it is involved in glycolysis; in mammals it is involved in gluconeogenesis; in plants in carbohydrate biosynthesis; in some bacteria it provides a gateway for fructose into the Entner-Doudouroff pathway. Besides its role as a glycolytic enzyme, mammalian PGI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. Mammalian PGI is also neuroleukin [3], a neurotrophic factor which supports the survival of various types of neurons. The sequence of PGI is conserved among diverse species ranging from bacteria to mammals and structures form a similar fold (see ,PDB:1IAT,) [4,5], comprised of two subdomains that each form an α-β-α sandwich, with the active site located in the ...
Phosphomannose isomerase is a zinc binding enzyme that catalyses the reversible isomerization of mannose 6-phosphate and fructose 6-phosphate. These substrates could exist in two conformations. They are covalently closed (cyclic form) in one conformation while a covalent bond is disrupted in the other linear form. The reaction most likely proceeds by binding of the cyclic form of substrate, conversion of its closed to open form, transfer of protons between atoms of the open form of substrate by a suitable base followed by its cyclisation to form the cyclic form of the product. Structure of phosphomannose isomerase from Salmonella typhimurium The ...
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8xia: X-ray analysis of D-xylose isomerase at 1.9 A: native enzyme in complex with substrate and with a mechanism-designed inactivator.
Ll_KARI is a representative of the 14% of the 643 KARI sequences with a six-residue β2αB loop. Whereas in 12- and seven-residue β2αB-loop KARIs the antepenultimate and ultimate residues are highly conserved, in six-loop KARIs the ultimate conserved serine is usually preceded by a positively charged residue at the penultimate position. We hypothesized that residues Lys52 and Ser53 of Ll_KARI were equivalent in function to residues Arg76 and Ser78 in Ec_IlvC. Ll_KARIDD variant with mutations Lys52Asp and Ser53Asp, however, expressed at an extremely low level and exhibited no measurable activity with either cofactor, which could be a result of the destabilizing effects of the two adjacent Asp residues. Similar results were obtained with Ll_KARIED. These two Asp mutations are separated by an additional residue in KARIs with the longer β2αB loops. The failed transfer of E. coli cofactor switch mutations to Ll_KARI suggests that KARIs with six-residue loops require a modified approach.. To ...
van Tilbeurgh, H., J. Jenkins, M. Chiadmi, J. Janin, S. J. Wodak, N. T. Mrabet, and A. M. Lambeir, Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 3. Changing metal specificity and the pH profile by site-directed mutagenesis., Biochemistry, vol. 31, issue 24, pp. 5467-71, 1992 Jun 23. ...
van Tilbeurgh, H., J. Jenkins, M. Chiadmi, J. Janin, S. J. Wodak, N. T. Mrabet, and A. M. Lambeir, Protein engineering of xylose (glucose) isomerase from Actinoplanes missouriensis. 3. Changing metal specificity and the pH profile by site-directed mutagenesis., Biochemistry, vol. 31, issue 24, pp. 5467-71, 1992 Jun 23. ...
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Several hits in gapped BLAST to lacA-related proteins, e.g. residues 4-150 are 43% similar to the enzyme from M.tuberculosis. Residues 5-151 are 40% similar to MG396, a predicted lacA/rpiB galactoside acetyltransferase. Other similarities involve hypothetical proteins and predicted phosphoriboisomerase B proteins (rpiB), e.g. residues 2-153 are 36% similar to RPIB_ECOLI. No significant similarities to T.pallidum or C.trachomatis ...
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InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites. We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their individual strengths to produce a powerful integrated database and diagnostic tool.
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Substance Name:Phosphate Buffered Saline 1X Sterile Solution. CAS Number:7647-14-5, 7447-40-7, 7558-79-4, 7778-77-0, 7732-18-5. ...
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Saccharomyces cerevisiae strains expressing D-xylose isomerase (XI) produce some of the highest reported ethanol yields from D-xylose. Unfortunately, most bacterial XIs that have been expressed in S. cerevisiae are either not functional, require additional strain modification, or have low affinity for D-xylose. This study analyzed several XIs from rumen and intestinal microorganisms to identify enzymes with improved properties for engineering S. cerevisiae for D-xylose fermentation. Four XIs originating from rumen and intestinal bacteria were isolated and expressed in a S. cerevisiae CEN.PK2-1C parental strain primed for D-xylose metabolism by over expression of its native D-xylulokinase. Three of the XIs were functional in S. cerevisiae, based on the strains ability to grow in D-xylose medium. The most promising strain, expressing the XI mined from Prevotella ruminicola TC2-24, was further adapted for aerobic and fermentative growth by serial transfers of D-xylose cultures under aerobic, and followed
Fosmidomycin is a phosphonic antibiotic which inhibits 1-deoxy-D-xylulose 5-phosphate reductoisomerase (Dxr), the first committed step of the non-mevalonate pathway of isoprenoid biosynthesis. In Mycobacterium tuberculosis Dxr is encoded by Rv2870c, and although the antibiotic has been shown to inhibit the recombinant enzyme [1], mycobacteria are intrinsically resistant to fosmidomycin at the whole cell level. Fosmidomycin is a hydrophilic molecule and in many bacteria its uptake is an active process involving a cAMP dependent glycerol-3-phosphate transporter (GlpT). The fact that there is no glpT homologue in the M. tuberculosis genome and the highly impervious nature of the hydrophobic mycobacterial cell wall suggests that resistance may be due to a lack of cellular penetration. We demonstrated that dxr (Rv2780c) is an essential gene in M. tuberculosis, since we could not delete the chromosomal copy unless a second functional copy was provided on an integrating vector. This confirmed that the
ribose-5-phosphate isomerage B (RpiB):Presented here is a series of crystal structures solved by the Seattle Structural Genomics Center for Infectious Disease (SSGCID) of ribose-5-phosphate isomerase B, or RpiB, from the pathogenic fungus, Coccidioides immitis. This parasite, which resides in the soil in certain parts of the western hemisphere, causes coccidioidomycosis, also known as Valley Fever. The disease is difficult to diagnose as it causes masses which mimics a lung tumor. Ribose-5-phosphate isomerase is an enzyme that catalyzes the conversion between ribose-5-phosphate and ribulose-5-phosphate. This family of enzymes naturally occurs in two distinct classes, RpiA and RpiB, which play, among others, an important role in the pentose phosphate pathway, which converts a type of glucose into other molecules. Although RpiB occurs predominantly in bacteria, the RpiB from this fungal pathogen contains high structural similarity to other known RpiB structures despite modest sequence similarity. The C.
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The catabolism of glucose and xylose was studied in a wild type and creA deleted (carbon catabolite de-repressed) strain of Aspergillus nidulans. Both strains were cultivated in bioreactors with either glucose or xylose as the sole carbon source, or in the presence of both sugars. In the cultivations on single carbon sources, it was demonstrated that xylose acted as a carbon catabolite repressor (xylose cultivations), while the enzymes in the xylose utilisation pathway were also subject to repression in the presence of glucose (glucose cultivations). In the wild type strain growing on the sugar mixture, glucose repression of xylose utilisation was observed; with xylose utilisation occurring only after glucose was depleted. This phenomenon was not seen in the creA deleted strain, where glucose and xylose were catabolised simultaneously. Measurement of key metabolites and the activities of key enzymes in the xylose utilisation pathway revealed that xylose metabolism was occurring in the creA ...
During cultivation on a mixture of xylose and glucose, Bacteroides xylanolyticus X5-1 showed neither diauxic growth nor a substrate preference. Xylose-limited continuous-culture cells were able to consume xylose and glucose both as single substrates and as mixed substrates without any lag phase. When glucose was the growth-limiting substrate, the microorganism was unable to consume xylose. However, in the presence of a small amount of glucose or pyruvate, xylose was utilized after a short lag phase. In glucose-limited cells, xylose isomerase was present at low activity but xylulose kinase activity could not be detected. On addition of a mixture of xylose and glucose, xylose isomerase was induced immediately and xylulose kinase was induced after about 30 min. The induction of the two enzymes was sensitive to chloramphenicol, showing de novo synthesis. Xylose uptake in glucose-grown cells was very low, but the uptake rate could be increased when incubated with a xylose-glucose mixture. The ...
Accepted name: L-rhamnose isomerase. Reaction: L-rhamnose = L-rhamnulose. For diagram of reaction click here.. Other name(s): rhamnose isomerase; L-rhamnose ketol-isomerase. Systematic name: L-rhamnose aldose-ketose-isomerase. Comments: Contains two divalent metal ions located at different metal-binding sites within the active site. The enzyme binds the closed ring form of the substrate and catalyses ring opening to generate a form of open-chain conformation that is coordinated to one of the metal sites. Isomerization proceeds via a hydride-shift mechanism. While the enzyme from the bacterium Escherichia coli is specific for L-rhamnose, the enzyme from the bacterium Pseudomonas stutzeri has broad substrate specificity and catalyses the interconversion of L-mannose and L-fructose, L-lyxose and L-xylulose, D-ribose and D-ribulose, and D-allose and D-psicose [2].. Links to other databases: BRENDA, EXPASY, GTD, KEGG, Metacyc, PDB, CAS registry number: 9023-84-1. References:. 1. Domagk, G.F. and ...