Fatty Acyl Transferase

Schweizer, Eckhart; Lerch, Irmgard; Kroeplin-Rueff, Luistraut; Lynen, Feodor

doi:10.1111/j.1432-1033.1970.tb01030.x

Cited by 38 publications

(12 citation statements)

References 22 publications

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“…The binding of the palmitoyl product to the active site of MPT also coordinates the MPT-dependent elongation and AT-dependent priming reactions by facilitating the uptake of an acetyl moiety at the moment of termination : While malonyl uptake is prevented due to the blocked MPT active site, ACP can be charged with a new primer at the AT (Engeser et al 1979). It should still be noted that the MPT does not measure the length of the acyl chain in a strict sense : The MPT is able to transfer saturated acyl chains of different chain lengths readily if they are offered as CoA-bound substrates, and these acyl chains can even be fed into the reaction cycle as efficient primers (Pirson et al 1973 ;Schweizer et al 1970). In addition, if the supply of substrates is limited, the formation of saturated acyl-CoA products with shorter chain lengths is promoted in the yeast FAS complex (Sumper et al 1969).…”

Section: Active Sites Linkers and Substrate Shuttling In Fungal Fasmentioning

confidence: 99%

Structure and function of eukaryotic fatty acid synthases

Maier

Leibundgut

Boehringer

et al. 2010

Quart. Rev. Biophys.

123

127

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Abstract. In all organisms, fatty acid synthesis is achieved in variations of a common cyclic reaction pathway by stepwise, iterative elongation of precursors with two-carbon extender units. In bacteria, all individual reaction steps are carried out by monofunctional dissociated enzymes, whereas in eukaryotes the fatty acid synthases (FASs) have evolved into large multifunctional enzymes that integrate the whole process of fatty acid synthesis. During the last few years, important advances in understanding the structural and functional organization of eukaryotic FASs have been made through a combination of biochemical, electron microscopic and X-ray crystallographic approaches. They have revealed the strikingly different architectures of the two distinct types of eukaryotic FASs, the fungal and the animal enzyme system. Fungal FAS is a 2Á6 MDa a 6 b 6 heterododecamer with a barrel shape enclosing two large chambers, each containing three sets of active sites separated by a central wheel-like structure. It represents a highly specialized micro-compartment strictly optimized for the production of saturated fatty acids. In contrast, the animal FAS is a 540 kDa X-shaped homodimer with two lateral reaction clefts characterized by a modular domain architecture and large extent of conformational flexibility that appears to contribute to catalytic efficiency.

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Section: Active Sites Linkers and Substrate Shuttling In Fungal Fasmentioning

confidence: 99%

Structure and function of eukaryotic fatty acid synthases

Maier

Leibundgut

Boehringer

et al. 2010

Quart. Rev. Biophys.

123

127

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“…After an incubation period of 15 min at room temperature the reaction was stopped by the addition of 1 ml H,O together with 0.3 ml 3 M trichloroacetic acid. Otherwise, the assay was performed as described previously [7].…”

Section: Enzyme Assaysmentioning

confidence: 99%

Malonyl and Palmityl Transferase-less Mutants of the Yeast Fatty-Acid-Synthetase Complex

et al. 1975

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146 independently isolated mutants of the fatty acid synthetase gene locus fas1 were subdivided into six different complementation groups. Three of these groups, Va, Vb and Vd, have not been described before. The mutant fatty acid synthetases isolated from representatives of complementation group Vb were specifically deficient in two component enzymes at the same time, the malonyl and palmityl transferases. Among more than 180 fas1 and fas2 mutants systematically screened for malonyl and palmityl transferase activities no mutant was found affected in only one of these two fatty acid synthetase component enzymes. From this it is concluded that both transfer reactions are catalyzed by the same enzyme. In any malonyl transferase‐less fatty acid synthetase, neither of the two known malonyl binding sites, i.e. enzyme‐bound pantetheine and the non‐thiol binding site, accepts malonate. This indicates that malonate is transferred to both groups by the same enzyme. So far, no acetyl transferase‐less fas mutants have been characterized. On the other hand, the mutants of two fas1 complementation groups, Va and Vd, though negative in overall fatty acid synthetase activity had no deficiency in any of the known component enzymes which can be tested in vitro. A possible interrelationship between both findings is discussed.

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“…The inhibition of fatty acid synthesis when longchain acyl-CoA derivatives are used as primers a t higher concentrations was recently also reported by Schweizer [30]. He interpreted the inhibition to be due to general and nonspecific inactivation of the enzyme complex, probably by a detergent-like effect.…”

Section: Derivatives Of Decanoyl-coa As Printermentioning

confidence: 56%

“…The fatty acid methyl esters wen separated on polyethylene glycol succinate (15O/,, 2 m) and silicone gum rubber (SE 30 …”

Section: Gas Chromatographymentioning

confidence: 99%

The Specificity of Yeast Fatty‐Acid Synthetase with Respect to the “Priming” Substrate

Pirson

Schuhmann

Lynen

1973

European Journal of Biochemistry

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Yeast fatty acid synthetase catalyzes the synthesis of palmityl-CoA and stearyl-CoA from acetyl-CoA and malonyl-CoA. Acetyl-CoA serves as "primer" of the reaction cycle. The specificity of the fatty acid synthetase with respect to the "priming" substrate was studied on the purified enzyme.1. I n its function as primer acetyl-CoA was replaced by homologous saturated acyl-CoA derivatives (butyryl-CoA, capronyl-CoA, etc.). I n these experiments nonanoyl-CoA and d ecanoylCoA were good primers in low concentration range. This kind of fatty acid synthesis leads to normal end products.2. At higher concentrations of priming substrate an inhibitory effect became apparent with all long-chain acyl-CoA derivatives. With decanoyl-CoA the degree of inhibition was dependent on the concentration of malonyl-CoA. This was interpreted as competition between decaiioyl-CoA and malonyl-CoA.3. The rate of synthesis with ~~-3-hydroxydecanoyl-CoA and A2-decenoyl-CoA as prtmer was 25-50 times slower than with decanoyl-CoA. The rate-limiting step was the transfer of the acyl residue from CoA to the enzyme. The saturated acids C,,-C,s were isolated as end prcsducts of this synthesis.4. Derivatives of deoanoyl-CoA with ciubstitutions a t positions more distant from the Icarboxyl group were not so strongly depressed i n their priming activity, e.g. d3-decenoyl-CoA or 4-0x0-decanoyl-CoA. I n these cases the functional groups were retained during chain elongation. As reaction products unsaturated acids or 0x0 acids respectively were isolated.5. The enzymatic reduction of the double bond (A3-decenoyl-CoA) or the 0x0 grou11 (4-0x0-decanoyl-CoA) could be demonstrated only as a slow side reaction.

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Fatty Acyl Transferase

Cited by 38 publications

References 22 publications

Structure and function of eukaryotic fatty acid synthases

Structure and function of eukaryotic fatty acid synthases

Malonyl and Palmityl Transferase-less Mutants of the Yeast Fatty-Acid-Synthetase Complex

The Specificity of Yeast Fatty‐Acid Synthetase with Respect to the “Priming” Substrate

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