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1.
Org Lett ; 3(19): 3045-7, 2001 Sep 20.
Article in English | MEDLINE | ID: mdl-11554839

ABSTRACT

The first enantioselective synthesis of the methyl ester of CPE, a potential intermediate in coronatine (COR) biosynthesis, is described. Comparison of the specific rotation of the synthetic ester with that of the methyl ester of natural CPE established that the latter possesses the (R) configuration. This configuration is the same as that found at the corresponding asymmetric center of coronatine. Structure: see text.


Subject(s)
Amino Acids/chemistry , Bacterial Toxins/chemistry , Cyclopentanes/chemical synthesis , Indenes/chemistry , Chromatography, High Pressure Liquid , Esters/chemistry , Fermentation , Molecular Conformation , Pseudomonas/chemistry , Stereoisomerism
2.
Gene ; 270(1-2): 191-200, 2001 May 30.
Article in English | MEDLINE | ID: mdl-11404016

ABSTRACT

Coronafacic acid (CFA) is the polyketide component of coronatine (COR), a phytotoxin produced by the plant pathogen Pseudomonas syringae. The CFA polyketide synthase (PKS) consists of two open reading frames (ORFs) that encode type I multifunctional proteins and several ORFs that encode monofunctional proteins. Sequence comparisons of the modular portions of the CFA PKS with other prokaryotic, modular PKSs elucidated the boundaries of the domains that are involved in the individual stages of polyketide assembly. The two beta-ketoacyl:acyl carrier protein synthase (KS) domains in the modular portion of the CFA PKS exhibit a high degree of similarity to each other (53%), but are even more similar to the KS domains of DEBS, RAPS, and RIF. Cfa6 possesses two acyltransferases- AT0, which is associated with a loading domain, and AT1, which uses ethylmalonyl-CoA (eMCoA) as a substrate for chain extension. Cfa7 contains an AT that uses malonyl-CoA as a substrate for chain extension. The Cfa6 AT0 shows 35 and 32% similarity to the DEBS1 and NidA1 AT0s, respectively, and 32 and 36% similarity to the Cfa6 and Cfa7 AT1s. Sequence motifs have previously been identified that correlate with AT substrates. The motifs in Cfa6 AT1 were found to correlate reasonably well with those predicted for methylmalonyl-CoA (mMCoA) ATs. The motifs in the AT of Cfa7 correlated more poorly with those predicted for MCoA ATs. Three ACP domains occur in the modular proteins of the COR PKS. The loading domain-associated ACP0 showed 38% similarity to the loading domain ACP0s of DEBS1 and NidA1 and 32-36% similarity to the two module-associated ACPs of the COR PKS. It exhibited a higher degree of similarity to the module-associated ACPs of RAPS. The two module-associated ACPs show 39% similarity to each other, but appear more closely related to module-associated ACP domains in RAPS and RIFS. Furthermore, the DH and KR domains of Cfa6 and Cfa7 show greater similarity to DH and KR domains in RAPS and RIFS than to each other. The CFA PKS includes a thioesterase domain (TE I) that resides at the C-terminus of Cfa7 and a second thioesterase, which exists as a separate ORF (Cfa9, a TE II). Analysis of a Cfa7 thioesterase mutant demonstrated that the TE domain is required for the production of CFA. The co-existence of TE domains within modular PKSs along with physically separated, monofunctional TEs (TE IIs) has been reported for a number of modular polyketide and non-ribosomal peptide synthases (NRPS). An analysis of the two types of thioesterases using Clustal X yielded a dendrogram showing that TE IIs from PKSs and NRPSs are more closely related to each other than to domain TEs from either PKSs or NRPSs. Furthermore, the dendrogram indicates that both types of TE IIs are more closely related to TE domains associated with PKSs than to TE domains in NRPSs. Finally, the overall % G+C content and the % G+C content at the third codon for all of the PKS genes in the COR cluster suggest that these genes may have been recruited from a gram-positive bacterium.


Subject(s)
Indenes/metabolism , Multienzyme Complexes/genetics , Acyl Carrier Protein/genetics , Acyltransferases/genetics , Amino Acid Sequence , Catalytic Domain/genetics , Molecular Sequence Data , Multienzyme Complexes/metabolism , Phylogeny , Pseudomonas/genetics , Pseudomonas/metabolism , Sequence Alignment , Sequence Homology, Amino Acid , Thiolester Hydrolases/genetics
3.
Org Lett ; 3(8): 1117-9, 2001 Apr 19.
Article in English | MEDLINE | ID: mdl-11348173

ABSTRACT

[structure: see text]. The stereospecificity of hydride transfer from NADPH to FAD catalyzed by VlmR, a flavin reductase from the valanimycin biosynthetic pathway has been determined. By using stereospecifically deuterated NADPH, it has been shown that the 4-pro R hydrogen of NADPH is transferred.


Subject(s)
Antibiotics, Antineoplastic/chemical synthesis , Azo Compounds/chemical synthesis , Flavin-Adenine Dinucleotide/chemistry , Hydrogen/metabolism , NADH, NADPH Oxidoreductases/chemistry , NADP/chemistry , Antibiotics, Antineoplastic/chemistry , Azo Compounds/chemistry , FMN Reductase , Models, Chemical
4.
J Mol Biol ; 282(4): 875-89, 1998 Oct 02.
Article in English | MEDLINE | ID: mdl-9743633

ABSTRACT

Structures of free, substrate-bound and product-bound forms of Escherichia coli xanthine-guanine phosphoribosyltransferase (XGPRT) have been determined by X-ray crystallography. These are compared with the previously determined structure of magnesium and sulphate-bound XPRT. The structure of free XGPRT at 2.25 A resolution confirms the flexibility of residues in and around a mobile loop identified in other PRTases and shows that the cis-peptide conformation of Arg37 at the active site is maintained in the absence of bound ligands. The structures of XGPRT complexed with the purine base substrates guanine or xanthine in combination with cPRib-PP, an analog of the second substrate PRib-PP, have been solved to 2.0 A resolution. In these two structures the disordered phosphate-binding loop of uncomplexed XGPRT becomes ordered through interactions with the 5'-phosphate group of cPRib-PP. The cyclopentane ring of cPRib-PP has the C3 exo pucker conformation, stabilised by the cPRib-PP-bound Mg2+. The purine base specificity of XGPRT appears to be due to water-mediated interactions between the 2-exocyclic groups of guanine or xanthine and side-chains of Glu136 and Asp140, as well as the main-chain oxygen atom of Ile135. Asp92, together with Lys115, could help stabilise the N7-protonated tautomer of the incoming base and could act as a general base to remove the proton from N7 when the nucleotide product is formed. The 2.6 A resolution structure of XGPRT complexed with product GMP is similar to the substrate-bound complexes. However, the ribose ring of GMP is rotated by approximately 24 degrees compared with the equivalent ring in cPRib-PP. This rotation results in the loss of all interactions between the ribosyl group and the enzyme in the product complex.


Subject(s)
Escherichia coli/enzymology , Pentosyltransferases/chemistry , Pentosyltransferases/metabolism , Amino Acid Sequence , Binding Sites , Crystallization , Crystallography, X-Ray , Electrons , Guanosine Monophosphate/metabolism , Hydrogen Bonding , Ligands , Magnesium/metabolism , Models, Molecular , Molecular Sequence Data , Oxygen/metabolism , Phosphates/metabolism , Protein Conformation , Protons , Purines/metabolism , Ribose/analogs & derivatives , Ribose/metabolism , Sulfates/metabolism , Water/metabolism
5.
Biochemistry ; 36(37): 11061-8, 1997 Sep 16.
Article in English | MEDLINE | ID: mdl-9333323

ABSTRACT

Activation of gluatmine phosphoribosylpyrophosphate (RPPP) amidotransferase (GPATase) by binding of a PRPP substrate analog results in the formation of a 20 A channel connecting the active site for glutamine hydrolysis in one domain with the PRPP site in a second domain. This solvent-inaccessible channel permits transfer of the NH3 intermediate between the two active sites. Tunneling of NH3 may be a common mechanism for glutamine amidotransferase-catalyzed nitrogen transfer and for coordination of catalysis at two distinct active sites in complex enzymes. The 2.4 A crystal structure of the active conformer of GPATase also provides the first description of an intact active site for the phosphoribosyltransferase (PRTase) family of nucleotide synthesis and salvage enzymes. Chemical assistance to catalysis is provided primarily by the substrate and secondarily by the enzyme in the proposed structure-based mechanism. Different catalytic and inhibitory modes of divalent cation binding to the PRTase active site are revealed in the active conformer of the enzyme and in a feedback-inhibited GMP complex.


Subject(s)
Amidophosphoribosyltransferase/metabolism , Ammonia/metabolism , Phosphoribosyl Pyrophosphate/metabolism , Amidophosphoribosyltransferase/chemistry , Binding Sites , Crystallography, X-Ray , Models, Chemical , Models, Molecular , Molecular Sequence Data , Protein Conformation
6.
J Biol Chem ; 272(37): 23303-11, 1997 Sep 12.
Article in English | MEDLINE | ID: mdl-9287340

ABSTRACT

The valanimycin producer Streptomyces viridifaciens contains a two-component enzyme system that catalyzes the oxidation of isobutylamine to isobutylhydroxylamine. One component of this enzyme system is isobutylamine hydroxylase, and the other component is a flavin reductase. The gene (vlmR) encoding the flavin reductase required by isobutylamine hydroxylase has been cloned from S. viridifaciens by chromosome walking. The gene codes for a protein of 194 amino acids with a calculated mass of 21,265 Da and a calculated pI of 10.2. Overexpression of the vlmR gene in Escherichia coli as an N-terminal His-tag derivative yielded a soluble protein that was purified to homogeneity. Removal of the N-terminal His-tag from the overexpressed protein by thrombin cleavage also produced a soluble protein. Both forms of the protein exhibited a high degree of flavin reductase activity, and the thrombin-cleaved form functioned in combination with isobutylamine hydroxylase to catalyze the conversion of isobutylamine to isobutylhydroxylamine. Kinetic data indicate that the overexpressed protein utilizes FAD and NADPH in preference to FMN, riboflavin, and NADH. The deduced amino acid sequence of the VlmR protein exhibited similarity to several other flavin reductases that may constitute a new family of flavin reductases.


Subject(s)
Anti-Bacterial Agents/biosynthesis , Bacterial Proteins , Genes, Bacterial , NADH, NADPH Oxidoreductases/genetics , Streptomyces/genetics , Amino Acid Sequence , Antibiotics, Antineoplastic/biosynthesis , Azo Compounds/chemical synthesis , Base Sequence , Chromosome Walking , Circular Dichroism , Cloning, Molecular , Escherichia coli/genetics , Flavins/metabolism , Kinetics , Mixed Function Oxygenases/metabolism , Molecular Sequence Data , NADH, NADPH Oxidoreductases/biosynthesis , Recombinant Proteins/biosynthesis , Sequence Analysis, DNA , Sequence Homology, Amino Acid , Spectrometry, Fluorescence , Streptomyces/enzymology , Substrate Specificity
7.
Arch Biochem Biophys ; 339(1): 47-54, 1997 Mar 01.
Article in English | MEDLINE | ID: mdl-9056232

ABSTRACT

Streptomyces viridifaciens MG456-hF10 produces the antitumor agent valanimycin, which is a member of a family of antibiotics containing the azoxy group. An enzyme involved in the biosynthesis of valanimycin has been purified 360-fold from S. viridifaciens. This enzyme, isobutylamine N-hydroxylase, catalyzes the oxidation of isobutylamine to isobutylhydroxylamine in the presence of oxygen and a reduced flavin cofactor. Unlike other known N-hydroxylases, isobutylamine N-hydroxylase cannot carry out the reduction of the flavin cofactor. Rather, the reduced flavin is supplied by a separate flavin reductase that is present in extracts of S. viridifaciens. The reduced flavin cofactor could also be supplied by the flavin mononucleotide reductase of Vibrio fischeri. The requirement for molecular oxygen and a reduced flavin indicates that the N-hydroxylase is a flavin monooxygenase and that the mechanism for the hydroxylation is likely to proceed via the formation of a flavin 4a-hydroperoxide. Isobutylamine N-hydroxylase exhibited a subunit molecular mass of 40 kDa and existed in dimeric or trimeric form depending upon buffer conditions. The pI of the protein was found to be ca. 5.1 and the enzyme exhibited a sensitivity to thiol-directed reagents.


Subject(s)
Mixed Function Oxygenases/isolation & purification , Streptomyces/enzymology , Amino Acid Sequence , Azo Compounds/metabolism , Bacterial Proteins/isolation & purification , Bacterial Proteins/metabolism , Catalase/metabolism , FMN Reductase , Molecular Sequence Data , Molecular Weight , NADH, NADPH Oxidoreductases/isolation & purification , Peptides/chemistry , Substrate Specificity
8.
J Bacteriol ; 179(4): 1385-92, 1997 Feb.
Article in English | MEDLINE | ID: mdl-9023226

ABSTRACT

Sparsomycin is an antitumor antibiotic produced by Streptomyces sparsogenes. Biosynthetic experiments have previously demonstrated that one component of sparsomycin is derived from L-tryptophan via the intermediacy of (E)-3-(4-oxo-6-methyl-5-pyrimidinyl)acrylic acid and (E)-3-(2,4-dioxo-6-methyl-5-pyrimidinyl)acrylic acid. An enzyme which catalyzes the conversion of (E)-3-(4-oxo-6-methyl-5-pyrimidinyl)acrylic acid to (E)-3-(2,4-dioxo-6-methyl-5-pyrimidinyl)acrylic acid has been purified 740-fold to homogeneity from S. sparsogenes. The molecular mass of the native and denatured enzyme was 87 kDa, indicating that the native enzyme is monomeric. The enzyme required NAD+ for activity but lacked rigid substrate specificity, since analogs of both NAD+ and 3-(4-oxo-6-methyl-5-pyrimidinyl)acrylic acid could serve as substrates. The enzyme was very weakly inhibited by mycophenolic acid. Monovalent cations were required for activity, with potassium ions being the most effective. The enzyme exhibited sensitivity toward diethylpyrocarbonate and some thiol-directed reagents, and it was irreversibly inhibited by 6-chloropurine. The properties of the enzyme suggest it is mechanistically related to inosine-5'-monophosphate dehydrogenase.


Subject(s)
Acrylates/metabolism , Antibiotics, Antineoplastic/biosynthesis , Oxygenases/metabolism , Pyrimidinones/metabolism , Sparsomycin/biosynthesis , Streptomyces/enzymology , Amino Acids/analysis , Cations/pharmacology , Diethyl Pyrocarbonate/pharmacology , Hypoxanthines/pharmacology , Isoelectric Point , Kinetics , Molecular Weight , Mycophenolic Acid/pharmacology , NAD/analogs & derivatives , NAD/metabolism , Oxygenases/antagonists & inhibitors , Oxygenases/chemistry , Oxygenases/isolation & purification , Purines/pharmacology , Substrate Specificity , Sulfhydryl Reagents/pharmacology
9.
J Bacteriol ; 179(2): 409-16, 1997 Jan.
Article in English | MEDLINE | ID: mdl-8990292

ABSTRACT

The flavoprotein isobutylamine N-hydroxylase (IBAH) catalyzes the oxidation of isobutylamine to isobutylhydroxylamine, a key step in the biosynthesis of the azoxy antibiotic valanimycin. By using oligonucleotide primers designed from peptide sequence information derived from native IBAH, a fragment of the gene (vlmH) encoding IBAH was amplified by PCR from a genomic library of the valanimycin-producing organism, Streptomyces viridifaciens MG456-hF10. The gene fragment was then employed as a probe to clone the entire vlmH gene from an S. viridifaciens genomic library. Overexpression of the vlmH gene in Escherichia coli gave a soluble protein that was purified to homogeneity. The purified protein exhibited the catalytic activity expected for IBAH. The deduced amino acid sequence of IBAH exhibited the greatest similarity to the Sox/DszC protein from Rhodococcus sp. strain IGT38, a flavoprotein involved in the oxidation of dibenzothiophene to the corresponding sulfone. Significant similarities were also found between the amino acid sequence of IBAH and those of the acyl coenzyme A dehydrogenases.


Subject(s)
Bacterial Proteins , Butylamines/metabolism , Mixed Function Oxygenases/genetics , Streptomyces/enzymology , Amino Acid Sequence , Animals , Azo Compounds/chemistry , Azo Compounds/metabolism , Base Sequence , Cloning, Molecular , DNA, Bacterial , Gene Expression , Humans , Mixed Function Oxygenases/metabolism , Molecular Sequence Data , Sequence Homology, Amino Acid , Streptomyces/genetics
10.
Bioorg Med Chem ; 4(7): 1077-88, 1996 Jul.
Article in English | MEDLINE | ID: mdl-8831979

ABSTRACT

The synthesis of cyclopentyl and cyclopentenyl analogues of the alpha-anomer of D-ribose-5-phosphate from D-ribonolactone and D-ribose is described. These analogues, which have the same absolute configuration as D-ribose-5-phosphate, were incubated with PRPP synthetases in an attempt to prepare the corresponding carbocyclic PRPP analogues. The carbocyclic ribose-5-phosphate analogues were found to be inhibitors, rather than substrates, for 5-phosphoribosyl alpha-1-pyrophosphate synthetases of both bacterial and human origin. The inhibitory behaviour of the analogues is described.


Subject(s)
Ribose-Phosphate Pyrophosphokinase/metabolism , Ribosemonophosphates/chemical synthesis , Humans , Hydrogen-Ion Concentration , Kinetics , Pyrimidine Nucleotides/metabolism , Ribosemonophosphates/metabolism , Salmonella typhimurium , Stereoisomerism
11.
J Biol Chem ; 270(29): 17394-9, 1995 Jul 21.
Article in English | MEDLINE | ID: mdl-7542237

ABSTRACT

Glutamine phosphoribosylpyrophosphate (PRPP) amidotransferase catalysis and regulation were studied using a new stable carbocyclic analog of PRPP, 1-alpha-pyrophosphoryl-2-alpha, 3-alpha-dihydroxy-4-beta-cyclopentane-methanol-5-phosphate (cPRPP). Although cPRPP competes with PRPP for binding to the catalytic C site of the Escherichia coli enzyme, two lines of evidence demonstrate that cPRPP, unlike PRPP, does not promote an active enzyme conformation. First, cPRPP was not able to "activate" Cys1 for reaction with glutamine or a glutamine affinity analog. The ring oxygen of PRPP may thus be necessary for the conformation change that activates Cys1 for catalysis. Second, binding of cPRPP to the C site blocks binding of AMP and GMP, nucleotide end product inhibitors, to this site. However, the binding of nucleotide to the allosteric site was essentially unaffected by cPRPP in the C site. Since it is expected that nucleotide inhibitors would bind with low affinity to the active enzyme conformation, the nucleotide binding data support the conclusion that cPRPP does not activate the enzyme.


Subject(s)
Amidophosphoribosyltransferase/metabolism , Glutamine/metabolism , Phosphoribosyl Pyrophosphate/pharmacology , Adenosine Monophosphate/metabolism , Amidophosphoribosyltransferase/antagonists & inhibitors , Binding, Competitive , Guanosine Monophosphate/metabolism , Hydrolysis , Phosphoribosyl Pyrophosphate/analogs & derivatives , Structure-Activity Relationship
12.
J Enzyme Inhib ; 8(4): 243-53, 1995.
Article in English | MEDLINE | ID: mdl-7542321

ABSTRACT

The enzyme S-adenosylhomocysteine hydrolase (E.C.3.3.1.1) occurs in two forms in bovine liver: Type A, which carries four moles of NAD+ per mole of enzyme tetramer, and Type B, which carries two moles of NAD+ per mole of tetramer. The inhibition of these two forms of the enzyme with 2',2'-difluoro-2'-deoxyadenosine has been investigated. The studies examined the binding stoichiometry and stability of the enzyme-inhibitor complexes formed from each type of the enzyme, the degree of NAD+ reduction and NAD+ release, and the possibility of covalent bond formation between the enzyme and the inhibitor. Significant differences in the behavior of the two forms of the enzyme were encountered which may have important implications for the design of S-adenosylhomocysteine hydrolase inhibitors as therapeutic agents.


Subject(s)
Deoxyadenosines/pharmacology , Hydrolases/antagonists & inhibitors , NAD/metabolism , Adenosylhomocysteinase , Animals , Cattle , Dose-Response Relationship, Drug , Enzyme Reactivators/metabolism , Enzyme Stability , Hydrolases/metabolism , Kinetics , Liver/enzymology , Models, Chemical , Protein Binding , S-Adenosylhomocysteine/metabolism , Time Factors
13.
J Antibiot (Tokyo) ; 45(7): 1161-6, 1992 Jul.
Article in English | MEDLINE | ID: mdl-1517161

ABSTRACT

Stable mutants that are blocked in the production of the polyketide antibiotic furanomycin were generated by treatment of Streptomyces threomyceticus (ATCC 15795) with a combination of N-methyl-N'-nitro-N-nitrosoguanidine (NTG) and ultraviolet light. On the basis of their cosynthetic properties in mixed culture, the mutants were grouped into eleven phenotypic classes. The polarity of the cosynthetic reactions for seven classes of mutants was revealed by filtrate feeding experiments. This allowed them to be arranged in the most probable linear sequence of metabolic blocks. One of the remaining groups of mutants exhibited no cosynthetic behavior and is believed to be blocked in a gene that regulates furanomycin biosynthesis.


Subject(s)
Amino Acids/analysis , Streptomyces/isolation & purification , Culture Media , Streptomyces/chemistry
14.
Biochemistry ; 30(41): 9988-97, 1991 Oct 15.
Article in English | MEDLINE | ID: mdl-1911790

ABSTRACT

The acetylenic analogue of adenosine 9-(5',6'-dideoxy-beta-D-ribo-hex-5'-ynofuranosyl)adenine has been synthesized, and its behavior as an inhibitor of bovine S-adenosylhomocysteine hydrolase has been examined. Incubation of the enzyme with excess inhibitor caused a time-dependent, irreversible inactivation of the enzyme that was accompanied by the reduction of two equivalents of NAD+ to NADH and the loss of the two remaining equivalents of NAD+. With use of radiolabeled inhibitor, it was established that 4 equiv of the acetylenic analog bind irreversibly to the enzyme and that 4 equiv were required to inactivate the enzyme completely. The inactivated enzyme could not be reactivated by incubation with NAD+. Denaturation studies revealed that 2 equiv of the inhibitor are bound more tightly to the enzyme than the remainder, suggesting the formation of a covalent linkage between the oxidized inhibitor and the enzyme. The putative covalent linkage was found to be acid sensitive but stable to mild base. The linkage could not be stabilized by treatment of the enzyme-inhibitor complex with either borohydride or cyanoborohydride. A Kl of 173 nM was measured for the inhibitor, making it one of the more potent inhibitors that have been reported. The enzyme used in these studies was isolated by modification of an affinity chromatography method reported by Narayanan and Borchardt [(1988) Biochim. Biophys. Acta 965, 22-28]. The affinity chromatography unexpectedly led to the isolation of two forms of the enzyme. The major form contained 4.0 mol of nucleotide cofactor/mol of enzyme tetramer, while the minor form carried only 2.0 mol/tetramer.


Subject(s)
Dideoxyadenosine/analogs & derivatives , Hydrolases/antagonists & inhibitors , Adenosine/analogs & derivatives , Adenosine/pharmacology , Adenosylhomocysteinase , Binding Sites/drug effects , Dideoxyadenosine/chemical synthesis , Dideoxyadenosine/pharmacology , Enzyme Activation/drug effects , Enzyme Stability , Hydrolases/drug effects , Hydrolases/isolation & purification , Kinetics , NAD/chemistry , Protein Denaturation
16.
J Acoust Soc Am ; 63(3): 940-53, 1978 Mar.
Article in English | MEDLINE | ID: mdl-670559

ABSTRACT

A compilation, from the original papers, is presented of the data on the acoustic properties (i.e., velocity and attenuation) of mammalian tissues in the megahertz range of frequencies used in medical ultrasonics. The actual values reported have been quoted to present a clear picture of the current state of knowledge in order to enable it to be assessed and to enable future workers to compare their own results directly. In the 20 years since the last such compilation, the progress in estimating the relative contributions of the animal species, the condition of the tissues, the temperature and frequency at which measurements were made, and the method of measurement to the observed variation has been small. It is hoped that this compilation together with summarizing tables will both be of practical use to the worker in the field and also encourage the establishment of a stronger body of fundamental information for the application of ultrasonics in biology and medicine.


Subject(s)
Mammals/physiology , Sonication , Ultrasonics , Absorption , Animals , Blood Physiological Phenomena , Connective Tissue/physiology , Humans , In Vitro Techniques , Methods , Muscles/physiology , Nerve Tissue/physiology , Skin Physiological Phenomena , Temperature , Time Factors
20.
Proc Natl Acad Sci U S A ; 72(5): 1681-83, 1975 May.
Article in English | MEDLINE | ID: mdl-1057163

ABSTRACT

The stereochemistry of the decarboxylation of trans-p-coumaric acid to 4-hydroxystyrene by Aerobacter aerogenes has been examined. The decarboxylation has been found to proceed with retention of the geometry about the trans-substituted double-bond.


Subject(s)
Cinnamates/metabolism , Enterobacter/metabolism , Hydroxy Acids/metabolism , Coumarins/metabolism , Magnetic Resonance Spectroscopy , Molecular Conformation , Phosphates/metabolism , Stereoisomerism , Styrenes/metabolism
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