Biomaterial Database

Biosynthesis of lipoic acid: characterization of the lipoic acid auxotrophs Escherichia coli W1485-lip2 and JRG33-lip9. 1993

M A Hayden, and I Y Huang, and G Iliopoulos, and M Orozco, and G W Ashley

Department of Chemistry and of Biochemistry, Northwestern University, Evanston, Illinois 60208.

The abilities of the Escherichia coli lipoic acid auxotrophs W1485-lip2 and JRG33-lip9 to grow on succinate medium in the presence of octanoate, 8-mercaptooctanoate, or 6-mercaptooctanoate have been determined. Both organisms are mutated in lipA. Neither organism can use octanoate or 6-mercaptooctanoate for production of lipoate, but the lip2 allele can use 8-mercaptooctanoate. Chromosomal DNA from the auxotrophs was amplified by PCR using primers derived from the DNA sequence of wild-type lipA and then sequenced. Both mutants contain single G/C to A/T mutations in lipA, resulting in conversion of Ser307 into Phe in W1485-lip2 and Glu195 into Lys in JRG33-lip9. These results support the hypothesis that lipA is involved in the sulfur insertion step(s) of lipoate biosynthesis and indicate that it is possible to selectively block formation of the C8-S bond through suitable mutation in lipA.

UI	MeSH Term	Description	Entries
D008063	Thioctic Acid	An octanoic acid bridged with two sulfurs so that it is sometimes also called a pentanoic acid in some naming schemes. It is biosynthesized by cleavage of LINOLEIC ACID and is a coenzyme of oxoglutarate dehydrogenase (KETOGLUTARATE DEHYDROGENASE COMPLEX). It is used in DIETARY SUPPLEMENTS.	Lipoic Acid,Alpha-Lipogamma,Alpha-Lipon Stada,Alpha-Liponsaure Sofotec,Alpha-Lippon AL,Alphaflam,Azulipont,Fenint,Juthiac,Liponsaure-ratiopharm,MTW-Alphaliponsaure,Neurium,Pleomix-Alpha,Pleomix-Alpha N,Thioctacid,Thioctacide T,Thiogamma Injekt,Thiogamma oral,Tromlipon,Verla-Lipon,alpha-Lipoic Acid,alpha-Liponaure Heumann,alpha-Liponsaure von ct,alpha-Vibolex,biomo-lipon,duralipon,espa-lipon,Acid, alpha-Lipoic,Alpha Lipogamma,Alpha Lipon Stada,Alpha Liponsaure Sofotec,Alpha Lippon AL,AlphaLipogamma,AlphaLipon Stada,AlphaLiponsaure Sofotec,AlphaLippon AL,Injekt, Thiogamma,Liponsaure ratiopharm,Liponsaureratiopharm,MTW Alphaliponsaure,MTWAlphaliponsaure,Pleomix Alpha,Pleomix Alpha N,PleomixAlpha,PleomixAlpha N,Verla Lipon,VerlaLipon,alpha Lipoic Acid,alpha Liponaure Heumann,alpha Liponsaure von ct,alpha Vibolex,alphaLiponaure Heumann,alphaLiponsaure von ct,alphaVibolex,biomo lipon,biomolipon,espa lipon,espalipon
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D009154	Mutation	Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.	Mutations
D002210	Caprylates	Derivatives of caprylic acid. Included under this heading are a broad variety of acid forms, salts, esters, and amides that contain a carboxy terminated eight carbon aliphatic structure.	Caprylate,Octanoates,Caprylic Acids,Octanoic Acids,Acids, Caprylic,Acids, Octanoic
D004269	DNA, Bacterial	Deoxyribonucleic acid that makes up the genetic material of bacteria.	Bacterial DNA
D004926	Escherichia coli	A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.	Alkalescens-Dispar Group,Bacillus coli,Bacterium coli,Bacterium coli commune,Diffusely Adherent Escherichia coli,E coli,EAggEC,Enteroaggregative Escherichia coli,Enterococcus coli,Diffusely Adherent E. coli,Enteroaggregative E. coli,Enteroinvasive E. coli,Enteroinvasive Escherichia coli
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001483	Base Sequence	The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.	DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D015247	Deoxyribonuclease HindIII	One of the Type II site-specific deoxyribonucleases (EC 3.1.21.4). It recognizes and cleaves the sequence A/AGCTT at the slash. HindIII is from Haemophilus influenzae R(d). Numerous isoschizomers have been identified. EC 3.1.21.-.	DNA Restriction Enzyme HindIII,Deoxyribonuclease BstFI,Deoxyribonuclease EcoVIII,Endonuclease HindIII,B Pertussis Restriction Enzyme I,BpeI Endonuclease,Endodeoxyribonuclease BpeI,Endonuclease Asp52I,Endonuclease BbrI,Endonuclease BpeI,Endonuclease BstFI,Endonuclease Cfr32I,Endonuclease ChuI,Endonuclease Eco65I,Endonuclease Eco98I,Endonuclease EcoVIII,Endonuclease Hin1076III,Endonuclease Hin173I,Endonuclease HinJCII,Endonuclease HinbIII,Endonuclease HinfII,Endonuclease HsuI,Endonuclease LlaCI,Endonuclease MkiI,LlaCI, Endonuclease
D016133	Polymerase Chain Reaction	In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.	Anchored PCR,Inverse PCR,Nested PCR,PCR,Anchored Polymerase Chain Reaction,Inverse Polymerase Chain Reaction,Nested Polymerase Chain Reaction,PCR, Anchored,PCR, Inverse,PCR, Nested,Polymerase Chain Reactions,Reaction, Polymerase Chain,Reactions, Polymerase Chain