Microbial biochemistry /

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Bibliographic Details
Author / Creator:Cohen, Georges N.
Imprint:Dordrecht ; Boston : Kluwer Academic, 2004.
Description:xv, 333 p. : ill. (some col.) ; 27 cm.
Language:English
Subject:
Format: Print Book
URL for this record:http://pi.lib.uchicago.edu/1001/cat/bib/5600957
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ISBN:1402015410
Notes:Includes bibliographical references and index.
Table of Contents:
  • Foreword
  • Introduction
  • Chapter I.. Bacterial growth
  • The lag phase
  • The exponential phase
  • Linear growth
  • The yield of growth
  • Variation of the growth rate at limiting carbon source concentrations
  • Continuous growth. The chemostat
  • Advantages of the continuous exponential culture
  • Diauxic growth
  • Chapter II.. The outer membrane of Gramnegative bacteria and the cytoplasmic membrane
  • The outer membrane of Gram-negative bacteria
  • The cytoplasmic membrane
  • Energy generation
  • Subunit composition of the ATP synthase
  • Chapter III.. Peptidoglycan synthesis
  • General structure
  • Assembly of the peptidoglycan unit
  • The membrane steps
  • Assembly of the murein sacculus
  • Penicillin sensitivity
  • Chapter IV.. Cellular permeability
  • Accumulation, crypticity, and selective permeability
  • [beta]-galactoside permease
  • Periplasmic binding proteins and ATP binding cassettes
  • Phosphotransferases. The PTS system
  • A few well-identified cases of specific cellular permeability
  • Porins
  • Iron uptake
  • Conclusion
  • Chapter V.. Allosteric enzymes
  • Allosteric inhibition and activation
  • Polymeric nature of allosteric enzymes. The model of Monod, Wyman and Changeux
  • An alternative model
  • Conclusion
  • Chapter VI.. Glycolysis, gluconeogenesis and glycogen synthesis
  • Glycogen degradation
  • Glycolysis
  • Regulation of phosphofructokinase in bacteria
  • Gluconeogenesis
  • Fructose bisphosphatase in microorganisms
  • Glycogen synthesis
  • Control of glycogen biosynthesis
  • Branching enzyme
  • Chapter VII.. The pentose phosphate and Entner-Doudoroff pathways
  • The pentose phosphate pathway
  • The enzymes of the oxidative phase
  • The enzymes of the non oxidative phase
  • Regulation of the pentose phosphate pathway
  • Chapter VIII.. The tricarboxylic acid cycle and the glyoxylate bypass
  • The origin of acetyl CoA: the pyruvate dehydrogenase complex
  • Overview of the tricarboxylic acid (TCA) cycle
  • Organization of the enzymes of the tricarboxylic acid cycle
  • The tricarboxylic acid cycle is a source of biosynthetic precursors
  • The anaplerotic glyoxylic pathway bypass
  • Chapter IX.. Biosynthesis of lipids
  • Biosynthesis of short chain fatty acids
  • Biosynthesis of long-chain fatty acids
  • Regulation of yeast fatty acid synthesis at the genetic level
  • Regulation of fatty acid synthesis in bacteria
  • Biosynthesis of triglycerides
  • Biosynthesis of phosphoglycerides
  • Cyclopropane fatty acid synthase (CFA synthase)
  • Chapter X.. The Archaea
  • The different types of extremophiles
  • Chemical characteristics of Archaea
  • Archaea: Fossil Record
  • Economic Importance of the Archaea
  • Chapter XI.. Methanogens and methylotrophs
  • A). Methanogens and Methanogenesis
  • B). Methylotrophs
  • C). Carboxydotrophs
  • Chapter XII.. Enzyme induction in catabolic systems
  • The specificity of induction
  • De novo synthesis of [beta]-galactosidase
  • Constitutive mutants
  • Pleiotropy of the constitutive mutants
  • The genetic control and the cytoplasmic expression of inducibility in the synthesis of [beta]-galactosidase in E. coli. The Lac repressor
  • Operators and operons
  • Chapter XIII.. Transcription. RNA polymerase
  • The synthesis of messenger RNA. The bacterial RNA polymerase
  • Termination of transcription in prokaryotes
  • Transcription termination and polyA tails
  • Chapter XIV.. Negative regulation
  • Induction is correlated with the synthesis of a specific messenger
  • Isolation of the Lac repressor
  • The lac operator is a DNA sequence
  • Chapter XV.. Enzyme repression in anabolic pathways
  • Description of the phenomenon
  • Isolation of derepressed (constitutive) mutants in biosynthetic pathways. The use of structural analogues
  • Replacement of methionine by selenomethionine in proteins
  • Chapter XVI.. Positive regulation
  • The promoter region
  • Role of cyclic AMP and of the CAP protein in the binding of RNA polymerase to the promoter region
  • The synthesis and degradation of cyclic AMP
  • How does glucose exert its inhibitory effect on E. coli [beta]-galactosidase synthesis?
  • Chapter XVII.. The ribosomes
  • The components of E. coli ribosomes
  • The ribosomes of eukaryotes and of archaea
  • Mechanistic aspects of translation of messenger RNA to protein by ribosomes
  • Chapter XVIII.. The genetic code, the transfer RNAs and the aminoacyl-tRNA-synthetases
  • The genetic code
  • The transfer RNAs
  • Chapter XIX.. Attenuation
  • General remarks on regulatory mechanisms
  • Chapter XX.. The biological fixation of nitrogen
  • Control of nitrogenase synthesis and activity
  • Chapter XXI.. How biosynthetic pathways have been established
  • Use of isotopes
  • Use of auxotrophic mutants
  • Enzymatic analysis
  • Chapter XXII.. The aspartic acid family of amino acids. Biosynthesis
  • The biosynthesis of aspartic acid and asparagine
  • Biosynthesis of lysine from aspartate semialdehyde in bacteria
  • The synthesis of dipicolinic acid, a substance present in the spores of Gram-positive bacilli
  • The reduction of aspartate semialdehyde to homoserine, the common precursor of methionine and threonine
  • Biosynthesis of methionine from homoserine
  • S-adenosylmethionine (SAM) biosynthesis
  • Biosynthesis of threonine from homoserine
  • Biosynthetic threonine dehydratase
  • Isoleucine biosynthesis
  • Summary of the biosynthetic pathway of the aspartate family of amino acids
  • Chapter XXIII.. Regulation of the biosynthesis of the amino acids of the aspartic acid family in Enterobacteriaceae
  • I.. A Paradigm of Isofunctional and Multifunctional Enzymes and of the Allosteric Equilibrium
  • Two aspartokinases in E. coli
  • The threonine-sensitive homoserine dehydrogenase of E. coli
  • Isolation of a mutant lacking the lysine-sensitive aspartokinase and of revertants thereof
  • Evidence that the threonine-sensitive aspartokinase and homoserine dehydrogenase of E. coli are carried by the same bifunctional protein
  • The binding of threonine to aspartokinase I-homoserine dehydrogenase I
  • The binding of pyridine nucleotides to aspartokinase I-homoserine dehydrogenase I
  • The effects of threonine on aspartokinase I-homoserine dehydrogenase I are not only due to direct interactions
  • The allosteric transition of aspartokinase I-dehydrogenase I
  • Aspartokinase II-homoserine dehydrogenase II
  • Aspartokinase III
  • From homoserine to methionine
  • From threonine to isoleucine
  • Multifunctional proteins
  • II.. Regulations at the Genetic Level
  • The threonine operon
  • Regulation of the lysine regulon at the genetic level
  • Regulation of methionine biosynthesis at the genetic level
  • The methionine repressor
  • The metR gene and its product
  • The regulation of isoleucine synthesis at the genetic level
  • Appendix. More on regulons
  • Chapter XXIV.. Other patterns of regulation of the synthesis of amino acids of the aspartate family
  • Concerted feedback inhibition of aspartokinase activity in Rhodobacter capsulatus (formerly Rhodopseudomonas capsulata)
  • Pseudomonads
  • Specific reversal of a particular feedback inhibition by other essential metabolites. The case of Rhodospirillum rubrum
  • The particular case of spore-forming bacilli
  • Some other cases
  • Conclusion
  • Chapter XXV.. Biosynthesis of the amino acids of the glutamic acid family and its regulation
  • I.. The biosynthesis of glutamine
  • II.. The biosynthesis of glutamate
  • III.. Biosynthesis of proline
  • IV.. The biosynthesis of arginine and polyamines
  • V.. The biosynthesis of lysine in yeasts and molds
  • Chapter XXVI.. Biosynthesis of amino acids derived from phosphoglyceric acid and pyruvic acid
  • I.. Biosynthesis of glycine and serine
  • II.. Biosynthesis of cysteine
  • III.. Biosynthesis of alanine
  • IV.. Biosynthesis of valine
  • V.. Biosynthesis of leucine
  • VI.. Regulation of valine, isoleucine and leucine biosynthesis
  • Chapter XXVII.. Selenocysteine and selenoproteins
  • Outlook
  • Enzymes containing selenocysteine
  • Biochemical function of the selenocysteine residue in catalysis
  • Chapter XXVIII.. Biosynthesis of aromatic amino acids and its regulation
  • I.. The common pathway (Shikimic pathway)
  • II.. Biosynthesis of phenylalanine and tyrosine from chorismic acid
  • III.. The biosynthesis of tryptophan from chorismic acid
  • IV.. Enterochelin (enterobactin) biosynthesis
  • Chapter XXIX.. The biosynthesis of histidine and its regulation
  • Regulation of histidine biosynthesis at the genetic level
  • Chapter XXX.. The biosynthesis of nucleotides
  • I.. The biosynthesis of pyrimidine nucleotides
  • II.. The biosynthesis of purine nucleotides
  • Chapter XXXI.. The biosynthesis of deoxyribonucleotides
  • The formation of deoxyribonucleoside diphosphates from ribose nucleoside diphosphates
  • The ribosenucleoside diphosphate (NDP) 'reductase system of E. coli
  • Regulation of the activity of ribonucleoside diphosphate reductase
  • dCMP deaminase and thymidylate synthase
  • dUTPase
  • The ribonucleoside phosphate reductase of other organisms
  • A ribonucleotide triphosphate reductase reaction in E. coli grown under anaerobic conditions
  • The synthesis of deoxyribonucleoside triphosphates. from the diphosphates
  • Organization of DNA precursor synthesis in eukaryotic cells
  • Chapter XXXII.. Biosynthesis of some water-soluble vitamins and of their coenzyme forms
  • Biosynthesis of thiamine and cocarboxylase
  • Control of thiamine biosynthesis
  • Biosynthesis of riboflavin
  • Biosynthesis of nicotinamide, NAD[superscript +] and NADP[superscript +]
  • Regulation of the biosynthesis of nicotinamide and its derivatives
  • NAD[superscript +] and the ADP-ribosylation of proteins
  • Biosynthesis of para-aminobenzoic acid, of folic acid and its derivatives
  • Biosynthesis of vitamin B6 pyridoxine, and of its derivatives, pyridoxal, pyridoxamine and pyridoxal phosphate
  • Biosynthesis of biotin, biotin CO[subscript 2], and biocytin
  • The biotin operon and its repressor
  • Biosynthesis of lipoic acid
  • Biosynthesis of pantothenate and Coenzyme A
  • The biosynthesis of inositol
  • Biosynthesis of pyrroloquinoline quinone
  • Chapter XXXIII.. Biosynthesis of carotene, vitamin A, sterols, ubiquinones and menaquinones
  • Synthesis of the common precursor
  • Synthesis of [beta]-carotene, carotenoids and vitamin A
  • Synthesis of sterols
  • The biosynthesis of ubiquinones and menaquinones
  • Chapter XXXIV.. Biosynthesis of the tetrapyrrole ring system
  • Synthesis of protoporphyrin
  • Synthesis of heme from protoporphyrin
  • Synthesis of chlorophyll from protoporphyrin
  • Biosynthesis of the phycobilin chromophores. Chromatic adaptation
  • A type of chromatic adaptation under conditions of sulfur starvation
  • Chapter XXXV.. Biosynthesis of cobalamins including vitamin B[subscript 12]
  • Cobinamide biosynthesis
  • From GDP-cobinamide to cobalamin
  • Chapter XXXVI.. Interactions between proteins and DNA
  • DNA-binding proteins
  • Study of the protein-DNA complexes
  • Some other types of DNA-binding proteins
  • Chapter XXXVII.. Evolution of biosynthetic pathways
  • Principles of protein evolution
  • Two theories for the evolution of biosynthetic pathways
  • The methionine and cysteine biosynthetic pathways
  • The threonine, isoleucine, cysteine and tryptophan biosynthetic pathways
  • The evolutionary pathway leading to the three isofunctional aspartokinases in Escherichia coli
  • The aspartokinase and homoserine dehydrogenase activities of microorganisms other than Enterobacteriaceae
  • Transmembrane facilitators
  • DNA-binding regulator proteins
  • Abbreviations
  • Subject Index