Biosynthesis of Triphosphoribosyl-dephospho-coenzyme A, the Precursor of the Prosthetic Group of Malonate Decarboxylase

Hoenke, Stefan; Wild, Markus; Dimroth, Peter

doi:10.1021/bi0011532

Cited by 17 publications

(21 citation statements)

References 22 publications

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“…However, the feature that is common to both types of malonate decarboxylase is the formation of malonyl-S-ACP by an exchange reaction of malonate with an acetyl group that is bound to an acyl-carrier protein, which yields acetate and subsequent decarboxylation with the regeneration of the acetyl-S-ACP. The specific acyl-carrier protein subunit with a covalently attached 2'-(5´-phosphoribosyl)-3'-dephosphoCoA prosthetic group is also known to be common to both types of the malonate decarboxylases Hoenke et al, 2000).…”

Section: Malonate Decarboxylasementioning

confidence: 99%

Malonate Metabolism: Biochemistry, Molecular Biology, Physiology, and Industrial Application

Kim¹

2002

BMB Reports

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Malonate is a three-carbon dicarboxylic acid. It is well known as a competitive inhibitor of succinate dehydrogenase. It occurs naturally in biological systems, such as legumes and developing rat brains, which indicates that it may play an important role in symbiotic nitrogen metabolism and brain development. Recently, enzymes that are related to malonate metabolism were discovered and characterized. The genes that encode the enzymes were isolated, and the regulation of their expression was also studied. The mutant bacteria, in which the malonatemetabolizing gene was deleted, lost its primary function, symbiosis, between Rhizobium leguminosarium bv trifolii and clover. This suggests that malonate metabolism is essential in symbiotic nitrogen metabolism, at least in clover nodules. In addition to these, the genes matB and matC have been successfully used for generation of the industrial strain of Streptomyces for the production of antibiotics.

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Section: Malonate Decarboxylasementioning

confidence: 99%

Malonate Metabolism: Biochemistry, Molecular Biology, Physiology, and Industrial Application

Kim¹

2002

BMB Reports

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“…However, alternate malonate decarboxylases with ACP as a component of the enzyme were discovered in Malonomonas rubra [5][6][7]20,[29][30][31]76) , Klebsiella pneumoniae 20,[32][33][34][35]78) , Acinetobacter calcoaceticus 8,24,43,49,50) , and P. fluorescens 8,24,44) , and molecular biology-based analyses concerning the enzyme reaction mechanism have been developed. In 1998, we reanalyzed the subunit composition of the Pseudomonas enzyme, and discovered subunits d and e in addition to subunits a, b, and g 14) .…”

Section: Reaction Mechanism Of Malonate Decarboxylasementioning

confidence: 99%

“…In the former from a microaerotolerant anaerobic bacterium, Malonomonas rubra, biotin carrier protein is responsible for the decarboxylation of malonyl-S-ACP [5][6][7]20,[29][30][31]76) . The enzymes from aerobic and facultatively anaerobic bacteria, Pseudomonas putida 11,13,14,83) , P. fluorescens 8,24,44) , Acinetobacter calcoaceticus 8,24,43,49,50) , and Klebsiella pneumoniae 20,[32][33][34][35]78) belong to the latter category. However, the prosthetic group is common to both categories of malonate decarboxylase, i.e., every enzyme contains ACP with a covalently attached 2'-(5''-phosphoribosyl)-3'-dephospho-CoA 6,20,50,78) (Fig.…”

Section: Reaction Mechanism Of Malonate Decarboxylasementioning

confidence: 99%

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Malonate Decarboxylase in Bacteria and Its Application for Determination of Intracellular Acyl-CoA Thioesters

Chohnan

Takamura

2004

Microb. Environ.

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Pseudomonas putida is able to grow on malonate as a sole source of carbon and energy. Malonate decarboxylase is a key enzyme catabolizing malonate to acetate and CO 2 . The enzyme consists of the five different subunits, a (60 kDa), b (33 kDa), g (28 kDa), d (13 kDa), and e (30 kDa). The smallest subunit d is an acyl-carrier protein (ACP) possessing 2'-(5"-phosphoribosyl)-3'-dephospho-CoA as a prosthetic group. Acylation of ACP is the initial step triggering the decarboxylation of malonate in a cyclic manner, i.e., the d subunit is activated to form acyl-S-ACP by the e subunit in the presence of acetyl-CoA or malonyl-CoA as an active acyl donor. The acetyl residue on the d subunit is replaced with malonate by the a subunit, and the malonyl residue subsequently undergoes decarboxylation by the subunits b and g, thereby regenerating acetyl-S-ACP. This unique cyclic reaction mechanism that amplifies acetate as its product in proportion to the amount of a given acetyl-CoA and/or malonyl-CoA is allows one to detect pmol levels of the CoA derivatives. Moreover, one can separately measure the three CoA molecular species, acetyl-CoA, malonyl-CoA, and nonesterified CoA (CoASH), by a combination of the elimination of acetyl-CoA with citrate synthetase (EC 4.1.3.7) or acetylation of CoASH with phosphate acetyltransferase (EC 2.3.1.8). The micromethod, named the acyl-CoA cycling method, is useful to define the rapid changes in vivo in the size and composition of the CoA pool. By this micromethod, it has been demonstrated that there is a remarkable difference in the size and composition of intracellular pools of CoASH and CoA thioesters between aerobic bacteria and facultatively anaerobic bacteria. It has also been revealed that the composition of CoA pools in facultatively anaerobic bacteria drastically changes within minuites in response to the quality and quantity of the carbon source in the medium, growth phase, pH, incubation temperature, osmotic stress, or antibiotics to inhibit energy yielding systems and fatty acid biosynthesis.

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“…CitX thus functions as holo-citrate lyase synthase [systematic name, 2Ј-(5Љ-triphosphoribosyl)-3Ј-dephospho-CoA:apo-citrate lyase 2Ј-(5Љ-phosphoribosyl)-3Ј-dephospho-CoA transferase]. The mechanism for the biosynthesis of the 2Ј-(5Љ-phosphoribosyl)-3Ј-dephospho-CoA prosthetic group is not unique for citrate lyase but, as shown in a parallel work, follows a very similar route in the case of malonate decarboxylase (13).…”

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Identification of a Gene Cluster in Klebsiella pneumoniae Which Includes citX , a Gene Required for Biosynthesis of the Citrate Lyase Prosthetic Group

et al. 2002

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The biosynthesis of the 2-(5؆-phosphoribosyl)-3-dephospho-coenzyme A (CoA) prosthetic group of citrate lyase (EC 4.1.3.6), a key enzyme of citrate fermentation, proceeds via the initial formation of the precursor 2-(5؆-triphosphoribosyl)-3-dephospho-CoA and subsequent transfer to apo-citrate lyase with removal of pyrophosphate. In Escherichia coli, the two steps are catalyzed by CitG and CitX, respectively, and the corresponding genes are part of the citrate lyase gene cluster, citCDEFXG. In the homologous citCDEFG operon of Klebsiella pneumoniae, citX is missing. A search for K. pneumoniae citX led to the identification of a second genome region involved in citrate fermentation which comprised the citWX genes and the divergent citYZ genes. The citX gene was confirmed to encode holo-citrate lyase synthase, whereas citW was shown to encode a citrate carrier, the third one identified in this species. The citYZ genes were found to encode a two-component system consisting of the sensor kinase CitY and the response regulator CitZ. Remarkably, both proteins showed >40% sequence identity to the citrate-sensing CitA-CitB two-component system, which is essential for the induction of the citrate fermentation genes in K. pneumoniae. A citZ insertion mutant was able to grow anaerobically with citrate, indicating that CitZ is not essential for expression of citrate fermentation genes. CitX synthesis was induced to a basal level under anaerobic conditions, independent of citrate, CitB, and CitZ, and to maximal levels during anaerobic growth with citrate as the sole carbon source. Similar to the other citrate fermentation enzymes, CitX synthesis was apparently subject to catabolite repression.Many species of enterobacteria, such as Klebsiella pneumoniae and Escherichia coli, are able to utilize citrate under anoxic, fermentative conditions. Whereas K. pneumoniae can grow with citrate as the sole carbon and energy source (for a review, see reference 6), E. coli is dependent on the presence of an oxidizable cosubstrate (18), due to the lack of oxaloacetate decarboxylase. The initial step in all known citrate fermentation pathways is the Mg 2ϩ -dependent cleavage of citrate to acetate and oxaloacetate, a reaction catalyzed by citrate lyase (2, 10, 33).In K. pneumoniae, the structural genes for citrate lyase are part of the citCDEFG operon, which is located divergent to citS (Fig. 1). The proteins deduced from citC, citD, citE, and citF are citrate lyase ligase and the ␥, ␤, and ␣ subunits of citrate lyase, respectively (7). The citC operon is induced under anoxic conditions in the presence of citrate and Na ϩ ions. Its expression is strictly dependent on the citrate-sensing CitACitB two-component regulatory system (8,16,20) and is subject to catabolite repression, presumably by the cyclic AMP receptor protein (19).In E. coli, a citCDEFXG gene cluster between 13.9 and 14.2 min (Fig. 1) that exhibited high similarity to the K. pneumoniae citrate lyase cluster (5) but differed by the presence of an additional gene, designated citX (...

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Biosynthesis of Triphosphoribosyl-dephospho-coenzyme A, the Precursor of the Prosthetic Group of Malonate Decarboxylase

Cited by 17 publications

References 22 publications

Malonate Metabolism: Biochemistry, Molecular Biology, Physiology, and Industrial Application

Malonate Metabolism: Biochemistry, Molecular Biology, Physiology, and Industrial Application

Malonate Decarboxylase in Bacteria and Its Application for Determination of Intracellular Acyl-CoA Thioesters

Identification of a Gene Cluster in Klebsiella pneumoniae Which Includes citX , a Gene Required for Biosynthesis of the Citrate Lyase Prosthetic Group

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