L-Carnitine (R-[-]-3-hydroxy-4-trimethylaminobutyrate) is found in both eukaryotic and prokaryotic cells and participates in diverse processes including long-chain fatty-acid transport and osmoprotection. The enzyme crotonobetainyl/gamma-butyrobetainyl-CoA:carnitine CoA-transferase (CaiB; E.C. 2.8.3.-) catalyzes the first step in carnitine metabolism, leading to the final product gamma-butyrobetaine. The crystal structures of Escherichia coli apo-CaiB, as well as its Asp169Ala mutant bound to CoA and to carnitinyl-CoA, have been determined and refined to 1.6, 2.4, and 2.4 A resolution, respectively. CaiB is composed of two identical circular chains that together form an intertwined dimer. Each monomer consists of a large domain, containing a Rossmann fold, and a small domain. The monomer and dimer resemble those of formyl-CoA transferase from Oxalobacter formigenes, as well as E. coli YfdW, a putative type-III CoA transferase of unknown function. The CoA cofactor-binding site is formed at the interface of the large domain of one monomer and the small domain from the second monomer. Most of the protein-CoA interactions are formed with the Rossmann fold domain. While the location of cofactor binding is similar in the three proteins, the specific CoA-protein interactions vary somewhat between CaiB, formyl-CoA transferase, and YfdW. CoA binding results in a change in the relative positions of the large and small domains compared with apo-CaiB. The observed carnitinyl-CoA product in crystals of the CaiB Asp169Ala mutant cocrystallized with crotonoyl-CoA and carnitine could result from (i) a catalytic mechanism involving a ternary enzyme-substrate complex, independent of a covalent anhydride intermediate with Asp169, (ii) a spontaneous reaction of the substrates in solution, followed by binding to the enzyme, or (iii) an involvement of another residue substituting functionally for Asp169, such as Glu23.
"Rather, its closest homologue with known function is CaiB of E. coli, a Class III acyl CoA transferase that donates acetyl CoA to carnitine when that amino acid is used as a terminal electron acceptor in anaerobic conditions. CaiB is a homo-dimer (Rangarajan et al., 2005), but DddD is ; twice the size of CaiB, and has a tandemly repeated domain structure that likely forms an 'intramolecular dimer'. Nevertheless, by analogy with the function of CaiB, it is predicted that DddD adds an acyl CoA moiety to DMSP, prior to its subsequent cleavage and release of DMS (Todd et al., 2007; Fig. 1). "
[Show abstract][Hide abstract] ABSTRACT: This paper describes the ddd genes that are involved in the production of the gas dimethyl sulphide from the substrate dimethylsulphoniopropionate (DMSP), an abundant molecule that is a stress protectant in many marine algae and a few genera of angiosperms. What is known of the arrangement of the ddd genes in different bacteria that can undertake this reaction is reviewed here, stressing the fact that these genes are probably subject to horizontal gene transfer and that the same functions (e.g. DMSP transport) may be accomplished by very different mechanisms. A surprising number of DMS-emitting bacteria are associated with the roots of higher plants, these including strains of Rhizobium and some rhizosphere bacteria in the genus Burkholderia. One newly identified strain that is predicted to make DMS is B. phymatum which is a highly unusual beta-proteobacterium that forms N(2)-fixing nodules on some tropical legumes, in this case, the tree Machaerium lunatum, which inhabits mangroves. The importance of DMSP catabolism and DMS production is discussed, not only in terms of nutritional acquisition by the bacteria but also in a speculative scheme (the 'messy eater' model) in which the bacteria may make DMS as an info-chemical to attract other organisms, including invertebrates and other plankton.
[Show abstract][Hide abstract] ABSTRACT: The 3-hydroxypropionate cycle has been proposed to operate as the autotrophic CO2 fixation pathway in the phototrophic bacterium Chloroflexus aurantiacus. In this pathway, acetyl coenzyme A (acetyl-CoA) and two bicarbonate molecules are converted to malate. Acetyl-CoA is regenerated
from malyl-CoA by l-malyl-CoA lyase. The enzyme forming malyl-CoA, succinyl-CoA:l-malate coenzyme A transferase, was purified. Based on the N-terminal amino acid sequence of its two subunits, the corresponding
genes were identified on a gene cluster which also contains the gene for l-malyl-CoA lyase, the subsequent enzyme in the pathway. Both enzymes were severalfold up-regulated under autotrophic conditions,
which is in line with their proposed function in CO2 fixation. The two CoA transferase genes were cloned and heterologously expressed in Escherichia coli, and the recombinant enzyme was purified and studied. Succinyl-CoA:l-malate CoA transferase forms a large (αβ)n complex consisting of 46- and 44-kDa subunits and catalyzes the reversible reaction succinyl-CoA + l-malate → succinate + l-malyl-CoA. It is specific for succinyl-CoA as the CoA donor but accepts l-citramalate instead of l-malate as the CoA acceptor; the corresponding d-stereoisomers are not accepted. The enzyme is a member of the class III of the CoA transferase family. The demonstration
of the missing CoA transferase closes the last gap in the proposed 3-hydroxypropionate cycle.
Journal of Bacteriology 05/2006; 188(7):2646-55. DOI:10.1128/JB.188.7.2646-2655.2006 · 2.81 Impact Factor
[Show abstract][Hide abstract] ABSTRACT: The phototrophic bacterium Chloroflexus aurantiacus uses the 3-hydroxypropionate cycle for autotrophic CO2 fixation. This cycle starts with acetyl-coenzyme A (CoA) and produces glyoxylate. Glyoxylate is an unconventional cell carbon
precursor that needs special enzymes for assimilation. Glyoxylate is combined with propionyl-CoA to β-methylmalyl-CoA, which
is converted to citramalate. Cell extracts catalyzed the succinyl-CoA-dependent conversion of citramalate to acetyl-CoA and
pyruvate, the central cell carbon precursor. This reaction is due to the combined action of enzymes that were upregulated
during autotrophic growth, a coenzyme A transferase with the use of succinyl-CoA as the CoA donor and a lyase cleaving citramalyl-CoA
to acetyl-CoA and pyruvate. Genomic analysis identified a gene coding for a putative coenzyme A transferase. The gene was
heterologously expressed in Escherichia coli and shown to code for succinyl-CoA:d-citramalate coenzyme A transferase. This enzyme, which catalyzes the reaction d-citramalate + succinyl-CoA → d-citramalyl-CoA + succinate, was purified and studied. It belongs to class III of the coenzyme A transferase enzyme family,
with an aspartate residue in the active site. The homodimeric enzyme composed of 44-kDa subunits was specific for succinyl-CoA
as a CoA donor but also accepted d-malate and itaconate instead of d-citramalate. The CoA transferase gene is part of a cluster of genes which are cotranscribed, including the gene for d-citramalyl-CoA lyase. It is proposed that the CoA transferase and the lyase catalyze the last two steps in the glyoxylate
Journal of Bacteriology 09/2006; 188(18):6460-8. DOI:10.1128/JB.00659-06 · 2.81 Impact Factor
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