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Reprint of journal in end pocket / vi, 158 leaves : photos., tables, graphs ; 30 cm. / Title page, contents and abstract only. The complete thesis in print form is available from the University Library. / Thesis (Ph.D.)--University of Adelaide, Dept. of Biochemistry, 1978

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by Eric Kwok Wai Tam. / Thesis (Ph.D.)--Chinese University of Hong Kong, 1996. / Includes bibliographical references. / Table of Contents --- p.i / Acknowledgement --- p.iv / Abstract --- p.v / Abbreviation --- p.vii / Part A / Enantiospecific Syntheses of Cyclohexane Oxides from (-)-Quinic Acid / Chapter 1. --- Synthetic Application of (-)-Quinic Acid --- p.1 / Chapter 1.1 --- Introduction --- p.1 / Chapter 1.2 --- Syntheses of Cyclohexane Derivatives --- p.2 / Chapter 1.2.1 --- Syntheses of Shikimic Acid (2) and its Derivatives --- p.2 / Chapter 1.2.2 --- "Syntheses of D-myo-Inositol 1,4,5-Trisphosphate (52) & its analog" --- p.15 / Chapter 1.2.3 --- Syntheses of Mycosporins --- p.17 / Chapter 1.2.4 --- Synthesis of (+)-Palitantin (76) --- p.19 / Chapter 1.2.5 --- "Synthesis of 2-Crotonyloxy-(4R,5R,6R)-4,5,6-trihydroxy- cyclohex-2-enone (COTC) (82)" --- p.20 / Chapter 1.2.6 --- Syntheses of Cyclophellitol (83) and its Diastereomers --- p.21 / Chapter 1.2.7 --- Syntheses of Pseudo-sugars and its Derivatives --- p.24 / Chapter 1.2.8 --- Syntheses of Aminocyclitol Antibiotics --- p.34 / Chapter 1.2.9 --- Syntheses of A-ring Precursor of Daunomycin --- p.36 / Chapter 1.2.10 --- "Synthesis of 19-nor-lα,25-Dihydroxyvitamin D3" --- p.38 / Chapter 1.2.11 --- Synthesis of Isoquinuclidines --- p.41 / Chapter 1.2.12 --- Synthesis of Cyclohexenyl Iodide: Taxol CD-ring Precursor --- p.44 / Chapter 1.2.13 --- Synthesis of C-20 to C-34 Segment of FK-506 --- p.46 / Chapter 1.2.14 --- Synthesis of the Hexahydrobenzofuran Subunit of Avermectins --- p.49 / Chapter 1.2.15 --- Synthesis of Bicyclic Core of Enediyne --- p.50 / Chapter 1.2.16 --- Syntheses of Two Enantiopure Derivatives of 4-Hydroxy-2-cyclohexone --- p.53 / Chapter 1.3 --- Synthesis of Homochiral Linear Molecules --- p.57 / Chapter 1.3.1 --- Syntheses of (3S)-Mevalonolactone and its Derivatives --- p.57 / Chapter 1.3.2 --- Synthesis of the Subunit in Maytansinoids --- p.58 / Chapter 1.3.3 --- Synthesis of (+)-Negamycin --- p.59 / Chapter 1.3.4 --- Syntheses of Hepoxilins B3 and its Stereoisomers --- p.61 / Chapter 1.3.5 --- Synthesis of C-21 to C-25 Fragment of FK-506 --- p.62 / Chapter 1.4 --- Synthesis of Cyclopentane Derivatives --- p.63 / Chapter 1.4.1 --- Synthesis of 11 α-Hydroxy-13-oxaprostanoic Acid --- p.65 / Chapter 1.4.2 --- Synthesis of (-)-Pentenomycin I --- p.66 / Chapter 1.4.3 --- Syntheses of Carbovir and its Derivatives --- p.66 / Chapter 1.5 --- Synthesis of Cycloheptane Derivatives --- p.68 / Chapter 1.6 --- Conclusion --- p.70 / References --- p.71 / Chapter 2. --- Introduction of Cyclohexane Oxides --- p.81 / Chapter 2.1 --- General Background --- p.81 / Chapter 2.2 --- Previous Syntheses of Cyclohexane Oxides --- p.86 / Chapter 2.2.1 --- Racemic Syntheses of Crotepoxide --- p.86 / Chapter 2.2.2 --- Racemic Syntheses of Senepoxide --- p.89 / Chapter 2.2.3 --- A Racemic Synthesis of Pipoxide --- p.92 / Chapter 2.2.4 --- Syntheses of Enantiopure Cyclohexane Oxides --- p.93 / References --- p.96 / Chapter 3. --- Retrosynthetic Analysis and Strategy --- p.99 / Chapter 3.1 --- Antithetic Analysis of Cyclohexane Oxides --- p.99 / Chapter 3.2 --- Problems Encounter in the Conversion of Diene into Cyclohexane Oxides --- p.100 / Chapter 3.3 --- Photo-oxygenation Approach to Cyclohexane Oxides --- p.102 / Chapter 3.4 --- Reasons for Choosing the Silyl Ether as Blocking Group --- p.104 / Chapter 3.5 --- Strategy for Synthesis of Diene 373 from Quinic acid --- p.105 / References --- p.106 / Chapter 4. --- Results and discussion --- p.108 / Chapter 4.1 --- Synthesis of Silyl Benzoate381 --- p.108 / Chapter 4.2 --- Synthesis of Alkene373 --- p.111 / Chapter 4.3 --- Syntheses of (+)-Crotepoxide (289)，(+)-Bosenepoxide (290) and (-)-iso-Crotepoxide (304) --- p.115 / Chapter 4.4 --- "Syntheses of the (+)-β-Senepoxide (295)，(+)-Pipoxide Acetate (365), (-) Tintanoxide (294) and (-)-Senepoxide (291)" --- p.121 / References --- p.124 / Chapter 5. --- Conclusion --- p.126 / Chapter 6. --- Experimental Section --- p.128 / References --- p.142 / Part B / Ruthenium Catalyzed cis-Dihydroxylation of Alkene / Chapter 1. --- Introduction --- p.143 / Chapter 1.1 --- Background --- p.143 / Chapter 1.2 --- General cis-Dihydroxylation Methods --- p.144 / Chapter 1.2.1 --- Potassium Permanganate (KMnO4) --- p.144 / Chapter 1.2.2 --- Osmium Tetraoxide (OsO4) --- p.146 / Chapter 1.3 --- Ruthenium Tetraoxide Oxidations --- p.148 / Chapter 1.4 --- Previous Reports of Using Ruthenium Tetraoxide (RuO4) Mediated syn-Dihydroxylation of Olefins --- p.149 / Chapter 1.4.1 --- The Snatzke and Fehlhaber Work --- p.149 / Chapter 1.4.2 --- The Sharpless and Akashi Work --- p.150 / Chapter 1.4.3 --- The Sica and Co-workers Work --- p.150 / References --- p.152 / Chapter 2. --- Ruthenium-Catalyzed cis-Dihydroxylation of Alkenes --- p.155 / Chapter 2.1 --- """Flash"" Dihydroxylation" --- p.155 / Chapter 2.2 --- "Stereochemical Outcome of ""Flash"" Dihydroxylation" --- p.155 / References --- p.157 / Chapter 3. --- Results and Discussion --- p.158 / Chapter 3.1 --- "Scope and Limitations of ""Flash"" Dihydroxylation" --- p.158 / Chapter 3.2 --- "Study of the Diastereoselectivity of ""Flash"" Dihydroxylation" --- p.168 / Chapter 3.3 --- "Study of Co-oxidants for ""Flash"" Dihydroxylation" --- p.170 / Chapter 3.4 --- "Solvent Effect for ""Flash"" Dihydroxylation" --- p.171 / Chapter 3.5 --- "Synthetic Application of ""Flash"" Dihydroxylation" --- p.173 / References --- p.175 / Chapter 4. --- Conclusion --- p.176 / Chapter 5. --- Experimental Section --- p.177 / References --- p.185 / Appendix --- p.186

Leung, Chi Yin. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2013. / Includes bibliographical references (leaves 81-89). / Electronic reproduction. Hong Kong : Chinese University of Hong Kong, [2012] System requirements: Adobe Acrobat Reader. Available via World Wide Web. / Abstracts also in Chinese.

The shikimate pathway is a primary metabolic pathway involved in the synthesis of aromatic compounds in plants, fungi, apicomplexan parasites and microbes. The absence of this pathway in animals makes it ideal for the synthesis of antimicrobial compounds and herbicides. Additionally, its branching into indole hormone synthesis and phenylpropanoid secondary metabolism makes this pathway attractive for metabolic engineering. Here, the focus is on the first step of the shikimate pathway catalyzed by DAHP synthase. This step consists of the condensation of phosphoenol pyruvate and erythrose-4-phosphate to make DAHP, which undergoes another six catalytic steps to synthesize chorismate, the precursor of the aromatic amino acids. Arabidopsis thaliana contains three DAHP synthase isozymes, which are known to indirectly regulate downstream pathways in response to wounding and pathogen stress. The model presented here proposes that DAHP synthase isozymes are regulated by the end products tyrosine, tryptophan and phenylalanine.

The shikimate pathway is a primary metabolic pathway involved in the synthesis of aromatic compounds in plants, fungi, apicomplexan parasites and microbes. The absence of this pathway in animals makes it ideal for the synthesis of antimicrobial compounds and herbicides. Additionally, its branching into indole hormone synthesis and phenylpropanoid secondary metabolism makes this pathway attractive for metabolic engineering. Here, the focus is on the first step of the shikimate pathway catalyzed by DAHP synthase. This step consists of the condensation of phosphoenol pyruvate and erythrose-4-phosphate to make DAHP, which undergoes another six catalytic steps to synthesize chorismate, the precursor of the aromatic amino acids. Arabidopsis thaliana contains three DAHP synthase isozymes, which are known to indirectly regulate downstream pathways in response to wounding and pathogen stress. The model presented here proposes that DAHP synthase isozymes are regulated by the end products tyrosine, tryptophan and phenylalanine.

Co-immunoprecipitation (co-IP) followed by proteomic analysis was employed to examine the phosphoenolpyruvate carboxylase (PEPC) interactome of developing castor oil seed (COS) endosperm. Earlier studies suggested that immunologically unrelated 107-kDa plant-type and 118-kDa bacterial-type PEPCs (p107/PTPC and p118/BTPC, respectively) are subunits of an unusual ~910-kDa hetero-octameric Class-2 PEPC complex of developing COS. The current results confirm that a tight physical interaction occurs between p118 and p107 since p118 quantitatively co-IP’d with p107 following elution of COS extracts through an anti-p107-IgG immunoaffinity column. No PEPC activity or immunoreactive PTPC or BTPC polypeptides were detected in the corresponding flow-through fractions. Although BTPCs lack the N-terminal phosphorylation site characteristic of PTPCs, Pro-Q Diamond Phosphoprotein staining, immunoblotting with phospho-(Ser/Thr) Akt substrate IgG, and phosphate-affinity PAGE demonstrated that the co-IP’d p118 was significantly phosphorylated at unique Ser and/or Thr residue(s). The co-IP of p118 and p107 was not influenced by their phosphorylation status. As p118 phosphorylation appeared unchanged 48 h following elimination of photosynthate supply due to COS depodding, the signaling mechanisms responsible for photosynthate-dependent p107 phosphorylation differ from those controlling p118’s in vivo phosphorylation. A third PEPC polypeptide of ~110-kDa (p110; RcPPC1) co-IP’d with p118 and p107 when depodded COS was used. Analysis of RcPpc1’s full-length cDNA sequence revealed p110’s identity with PTPCs, but that a pair of unique amino-acid substitutions occurs in its N-terminal sequence that may render p110 non-phosphorylatable in vivo. The plastidial pyruvate dehydrogenase complex (PDCpl) was identified as a novel PEPC interactor. Subcellular fractionation indicated that p118 and p107 are strictly cytosolic, but that PDCpl is targeted to both the cytosol and leucoplast of developing COS. Thus, a putative cytosolic metabolon involving PEPC and PDCpl could function to channel carbon from phosphoenolpyruvate to acetyl-CoA and/or to recycle CO2 from PDCpl to PEPC. / Thesis (Master, Biology) -- Queen's University, 2007-09-26 15:57:52.216

Abstract Maintenance of the mitochondrial respiratory chain complexes plays crucial role for the aerobic metabolism of the eukaryotes such as unicellular yeasts, for example, Saccharomyces cerevisiae as well as of human being. Mitochondrial respiratory function has been studied using the yeast S. cerevisiae as a model organism. Since yeast cells are also able to grow without respiration by fermentation, identification of the nuclear genes linked to respiratory function is possible by generation of nuclear gene deletions and testing for respiration-deficient phenotype of the yeast deletion strains id est for yeast cells only poorly or not at all growing on the media containing non-fermentable carbon sources. This study reports identification of a novel mitochondrial 2-enoyl thioester reductase from the yeasts Candida tropicalis and S. cerevisiae, Etr1p and Mrf1p, respectively. Examination of the function of these proteins in the respiration-deficient mrf1Δ strain from S. cerevisiae suggests that the reductase is involved in mitochondrial fatty acid synthesis (FAS type II) in the yeast. Site-directed mutagenesis of a conserved tyrosine in the catalytic site of the enzyme indicated that the 2-enoyl thioester reductase activity is critical for mitochondrial respiratory competence. In addition, subcellular localization to mitochondria was required for the complementation of the respiration-deficient phenotype of the yeast reductase deletion strain. The crystal structure for the Etr catalytic site mutant indicated the structural integrity of the mutant supporting the requirement of the tyrosine for the catalysis. Characterization of Etr crystal structures both in apo- and holo-forms containing NADPH established Etr as a member of novel subfamily of enoyl thioester reductases in the superfamily of medium-chain dehydrogenases/reductases (MDR). Two isoforms of Etr with the difference in three amino acids only are encoded by two distinct genes in C. tropicalis, whereas only single gene encodes the reductase functioning in the mitochondria in S. cerevisiae. The presence of two genes in C. tropicalis was taken as an example of genetic redundancy in this yeast, the two genes also shown to be expressed in slightly different ways under various carbon sources available for growth.

Call number: LD2668 .T4 1979 M34 / Master of Science