A rapid method for the preparation of pure heavy enzyme of gramicidin S synthetase

Christiansen, C.; Aarstad, Kjell; Zimmer, T.L.; Laland, S.

doi:10.1016/0014-5793(77)80942-3

Cited by 16 publications

(5 citation statements)

References 9 publications

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“…9). These results have recently been confirmed by CHRISTIANSEN et al [62] for gramicidin S synthetase 2. of tyrccidine and gramicidin S, one would have expected a corresponding analogy of the enzyme systems. The fact that they are not alike is not necessarily a contradiction because there is not sufficient information at the present time about the intracellular condition of these multienzymes or about their in vivo regulation.…”

Section: Biosynthesis Of Peptide Antibioticssupporting

confidence: 71%

Antibiotic Polypeptides – Biosynthesis on Multifunctional Protein Templates

Kleinkauf¹

1979

Planta Med

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Section: Biosynthesis Of Peptide Antibioticssupporting

confidence: 71%

Antibiotic Polypeptides – Biosynthesis on Multifunctional Protein Templates

Kleinkauf¹

1979

Planta Med

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“…Purification of Both Enzymes of Gramicidin S Synthetase. Gramicidin S synthetase was purified by a combination of procedures published by several authors (Koischwitz & Kleinkauf, 1976; Vater & Kleinkauf, 1976;Christiansen et al, 1977;Altmann et al, 1978).…”

Section: Methodsmentioning

confidence: 99%

“…The protein was eluted with the same buffer at a flow rate of 100 mL/h. Both components of gramicidin S synthetase were separated completely by this procedure (Christiansen et al, 1977).…”

Section: Methodsmentioning

confidence: 99%

Gramicidin S synthetase. Temperature dependence and thermodynamic parameters of substrate amino acid activation reactions

Vater¹,

Mallow²,

Gerhardt³

et al. 1985

Biochemistry

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In the biosynthesis of the cyclic decapeptide antibiotic gramicidin S, the constituent amino acids are activated by a two-step mechanism involving aminoacyl adenylate and thio ester formation which are both reversible processes. The dissociation constants (KD) for the gramicidin S synthetase-substrate amino acid-thio ester complexes are 100-1000-fold lower compared to the KM data of the preceding aminoacyl adenylate reactions. The affinity for these substrates is appreciably higher at the thio template sites than at the aminoacyl adenylate reaction centers. Therefore, the activation equilibria are quantitatively shifted toward thio ester formation. A set of thermodynamic parameters for the activation processes was determined from the temperature dependence of the KM and KD data. Reaction enthalpies were obtained from a van't Hoff analysis of these constants. delta G degree for the substrate activation reactions of the heavy enzyme of gramicidin S synthetase (GS 2) is predominantly controlled by entropy contributions. In contrast, the overall activation and concomitant racemization of phenylalanine by phenylalanine racemase (GS 1) are exothermic processes which are distinguished by a small negative reaction entropy.

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“…Because of the presence of o in the modified Eq. (1.1) the modified system requires a somewhat more complicated analysis than presented here [8].…”

Section: Formulation Of the Problemmentioning

confidence: 97%

On two methods for elimination of non-unique solutions of an integral equation with logarithmic kernel/^†

Christiansen

1982

Applicable Analysis

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A rapid method for the preparation of pure heavy enzyme of gramicidin S synthetase

Cited by 16 publications

References 9 publications

Antibiotic Polypeptides – Biosynthesis on Multifunctional Protein Templates

Antibiotic Polypeptides – Biosynthesis on Multifunctional Protein Templates

Gramicidin S synthetase. Temperature dependence and thermodynamic parameters of substrate amino acid activation reactions

On two methods for elimination of non-unique solutions of an integral equation with logarithmic kernel/^†

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A rapid method for the preparation of pure heavy enzyme of gramicidin S synthetase

Cited by 16 publications

References 9 publications

Antibiotic Polypeptides – Biosynthesis on Multifunctional Protein Templates

Antibiotic Polypeptides – Biosynthesis on Multifunctional Protein Templates

Gramicidin S synthetase. Temperature dependence and thermodynamic parameters of substrate amino acid activation reactions

On two methods for elimination of non-unique solutions of an integral equation with logarithmic kernel/†

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On two methods for elimination of non-unique solutions of an integral equation with logarithmic kernel/^†