The Si-C-F(-H) System

Haase, Vera; Kirschstein, Gerhard; List, Hildegard; Ruprecht, Sigrid; Sangster, Raymond; Schröder, Friedrich; Töpper, Wolfgang; Vanecek, Hans; Heit, Werner; Schlichting, J.; Katscher, Hartmut

doi:10.1007/978-3-662-06994-3_6

Cited by 2 publications

(2 citation statements)

References 7 publications

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“…It is important to know the tertiary structure of an enzyme for the investigation of its catalytic mechanism. The structures of the biotin-dependent carboxylases have been investigated by electron microscopy, and the overall shapes of transcarboxylase (reviewed in [14]), propionyl-CoA carboxylase [15], pyruvate carboxylase [16] and acetyl-CoA carboxylase [17] have been reported, although the details of the tertiary structures of the enzymes have not been determined.…”

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confidence: 99%

Molecular evolution of biotin‐dependent carboxylases

Toh

Kondo

Tanabe

1993

European Journal of Biochemistry

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Amino-acid sequences of three functional units from various biotin-dependent carboxylases, biotin carboxylase, biotin-carboxyl-carrier protein and carboxyl transferase, were investigated by computer-assisted sequence comparison to obtain information about the structure, function, and molecular evolution of the enzymes. Biotin-dependent carboxylases, except transcarboxylase and oxaloacetate decarboxylase which lack biotin carboxylase, exert their catalytic activities through the three functional units. The three functional units correspond with functional domains or subunits of the enzymes, and the genetic information for the units is encoded in different ways from enzyme to enzyme. It is known that biotin carboxylase is homologous to carbamoyl-phosphate synthetase, and that the biotin-carboxyl-carrier protein is homologous to lipoic-acid-binding domain. The evolutionary relationships between the functional units and their homologues were described. A model for the evolutionary history of the enzymes was proposed by molecular phylogenetic analysis, which shows how a wide variety of domain andor subunit structures for the enzymes may have been established. A repeated structure was found in biotin-carboxyl-carrier protein, and the secondary structure of the protein was predicted using the observed sequence similarity with a lipoic-acidbinding domain.The biotin-dependent carboxylases constitute a diverse group of enzymes, which includes acetyl-CoA carboxylase, propionyl-CoA carboxylase, oxaloacetate decarboxylase, pyruvate carboxylase and transcarboxylase. The enzymes are involved in a variety of essential metabolic pathways such as lipogenesis, gluconeogenesis and amino-acid metabolism. In addition, these enzymes have been identified in animals,

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confidence: 99%

Molecular evolution of biotin‐dependent carboxylases

Toh

Kondo

Tanabe

1993

European Journal of Biochemistry

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“…The same enzyme preparation carboxylates also acetyl-CoA to malonyl-CoA. In Mycobacterium phlei [7], Streptomyces noursei [8], Saccharomyces cerevisiae [10] and Mycobacterium smegmatis [15] only one enzyme is postulated which is able to carboxylate both acyl-CoAs. If it is supposed that also in Nocardia mediterranei only one enzyme exists for the transformation of propionyl-and acetyl-CoA 215 then propionyl-CoA is catalyzed nearly ten times faster than acetyl-CoA.…”

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confidence: 99%

Propionyl-CoA carboxylase in Nocardia mediterranei

Gygax¹

1984

FEMS Microbiology Letters

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The propionyl-CoA carboxylase activity of crude extracts of Nocardia mediterranei fractionated by ammonium sulfate (40-60%) is described. Such an enzyme may play an important role in the biosynthesis of rifamycin as well as in the degradation of various amino acids. The effect of different compounds on the enzymatic reaction have been investigated. Product P8/1-OG and citrate inhibited the enzyme. An activation by the amino acids isoleucine, methionine, threonine and valine was found. The results do not exclude that the same enzyme is responsible for the carboxylation of acetyl-CoA and propionyl-CoA.

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The Si-C-F(-H) System

Cited by 2 publications

References 7 publications

Molecular evolution of biotin‐dependent carboxylases

Molecular evolution of biotin‐dependent carboxylases

Propionyl-CoA carboxylase in Nocardia mediterranei

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