尿苷-5′-二磷酸葡萄糖焦磷酸化酶 来源于面包酵母
尿苷-5′-二磷酸葡萄糖焦磷酸化酶 来源于面包酵母结构式
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常用名 | 尿苷-5′-二磷酸葡萄糖焦磷酸化酶 来源于面包酵母 | 英文名 | Uridine-5'-diphosphoglucose pyrophosphorylase |
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| CAS号 | 9026-22-6 | 分子量 | N/A | |
| 密度 | N/A | 沸点 | N/A | |
| 分子式 | N/A | 熔点 | N/A | |
| MSDS | 美版 | 闪点 | N/A |
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Initial characterization of the human central proteome.
BMC Syst. Biol. 5 , 17, (2011) On the basis of large proteomics datasets measured from seven human cell lines we consider their intersection as an approximation of the human central proteome, which is the set of proteins ubiquitously expressed in all human cells. Composition and properties... |
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The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res. 14 , 2121-7, (2004) The National Institutes of Health's Mammalian Gene Collection (MGC) project was designed to generate and sequence a publicly accessible cDNA resource containing a complete open reading frame (ORF) for every human and mouse gene. The project initially used a r... |
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Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
Sci. Signal. 3(104) , ra3, (2010) Eukaryotic cells replicate by a complex series of evolutionarily conserved events that are tightly regulated at defined stages of the cell division cycle. Progression through this cycle involves a large number of dedicated protein complexes and signaling path... |
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Lysine acetylation targets protein complexes and co-regulates major cellular functions.
Science 325(5942) , 834-40, (2009) Lysine acetylation is a reversible posttranslational modification of proteins and plays a key role in regulating gene expression. Technological limitations have so far prevented a global analysis of lysine acetylation's cellular roles. We used high-resolution... |
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System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
Sci. Signal. 4(164) , rs3, (2011) To elucidate cellular events underlying the pluripotency of human embryonic stem cells (hESCs), we performed parallel quantitative proteomic and phosphoproteomic analyses of hESCs during differentiation initiated by a diacylglycerol analog or transfer to medi... |
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Structural basis for the broad substrate range of the UDP-sugar pyrophosphorylase from Leishmania major.
J. Mol. Biol. 405(2) , 461-78, (2011) Nucleotide sugars and the enzymes that are responsible for their synthesis are indispensable for the production of complex carbohydrates and, thus, for elaboration of a protective cellular coat for many organisms such as the protozoan parasite Leishmania. The... |
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The UDP-glucose pyrophosphorylase from Giardia lamblia is redox regulated and exhibits promiscuity to use galactose-1-phosphate.
Biochim. Biophys. Acta 1850(1) , 88-96, (2015) Giardia lamblia is a pathogen of humans and other vertebrates. The synthesis of glycogen and of structural oligo and polysaccharides critically determine the parasite's capacity for survival and pathogenicity. These characteristics establish that UDP-glucose ... |
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Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis.
Biochim. Biophys. Acta 1850(1) , 13-21, (2015) Mycobacterium tuberculosis is a pathogenic prokaryote adapted to survive in hostile environments. In this organism and other Gram-positive actinobacteria, the metabolic pathways of glycogen and trehalose are interconnected.In this work we show the production,... |
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Substrate kinetics and substrate effects on the quaternary structure of barley UDP-glucose pyrophosphorylase.
Phytochemistry 79 , 39-45, (2012) UDP-Glc pyrophosphorylase (UGPase) is an essential enzyme responsible for production of UDP-Glc, which is used in hundreds of glycosylation reactions involving addition of Glc to a variety of compounds. In this study, barley UGPase was characterized with resp... |
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Characterization of recombinant UDP- and ADP-glucose pyrophosphorylases and glycogen synthase to elucidate glucose-1-phosphate partitioning into oligo- and polysaccharides in Streptomyces coelicolor.
J. Bacteriol. 194(6) , 1485-93, (2012) Streptomyces coelicolor exhibits a major secondary metabolism, deriving important amounts of glucose to synthesize pigmented antibiotics. Understanding the pathways occurring in the bacterium with respect to synthesis of oligo- and polysaccharides is of relev... |