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球形红假单胞菌中5-氨基乙酰丙酸合成酶活性的调控

Control of 5-aminolaevulinate synthetase activity in Rhodopseudomonas spheroides.

作者信息

Wider de Xifra E A, Sandy J D, Davies R C, Neuberger A

出版信息

Philos Trans R Soc Lond B Biol Sci. 1976 Feb 5;273(924):79-98. doi: 10.1098/rstb.1976.0002.

Abstract

Rhodopseudomonas spheroides can grow in a defined medium with either light or oxygen as an energy source. Cells grown anaerobically or at very low oxygen tensions are rich in the photosynthetic pigment bacteriochlorophyll, whereas this pigment is virtually absent in cells grown under high oxygen tensions. Aminolaevulinate synthetase, the first enzyme on the pathway to bacteriochlorophyll, appears to play an important role in the control of bacteriochlorophyll synthesis. Thus, the enzyme has a high activity in extracts of pigmented cells and a low activity in extracts of non-pigmented cells. Further, oxygenation of a pigmented culture causes immediate cessation of pigment synthesis and produces a rapid fall in the activity of aminolaevulinate synthetase. This loss of activity appears to be due to the loss of an endogenous activator of the enzyme. Thus, pigmented cells contain cystine trisulphide, which at muM concentrations is an activator of aminolaevulinate synthetase, while oxygenation causes a rapid fall in the cellular content of this trisulphide. Cystathionase (EC 4.2.1.15) extracted from pigmented cells can catalyse the formation of cystine trisulphide from cystine, while rhodanese (EC 2.8.1.1) extracted from the same cells can catalyse the degradation of cystine trisulphide in the presence of sulphite to form cystine and thiosulphate. It is proposed that the cellular content of cystine trisulphide is controlled by changes in the levels of substrates for cystathionase and possibly rhodanese rather than changes in the amounts of these enzymes. Cystine trisulphide controls the activity of aminolaevulinate synthetase by converting a low-activity form of the enzyme (b-form) into a high-activity form (a-form). The fall in aminolaevulinate synthetase activity on oxygenation appears to be the result of cessation of conversion of b-form into a-form, along with a conversion of a-form into b-form. Factors affecting the equilibrium between the forms and the possible mechanisms for their interconversion are discussed.

摘要

球形红假单胞菌能够在一种特定培养基中生长,该培养基可以以光或氧气作为能源。在厌氧条件下或极低氧张力下生长的细胞富含光合色素细菌叶绿素,而在高氧张力下生长的细胞中几乎不存在这种色素。氨基乙酰丙酸合成酶是细菌叶绿素合成途径中的首个酶,它似乎在细菌叶绿素合成的调控中发挥着重要作用。因此,该酶在有色素细胞的提取物中具有高活性,而在无色素细胞的提取物中活性较低。此外,对有色素培养物进行氧合会导致色素合成立即停止,并使氨基乙酰丙酸合成酶的活性迅速下降。这种活性丧失似乎是由于该酶的一种内源性激活剂的丧失。因此,有色素细胞含有三硫化胱氨酸,在微摩尔浓度下它是氨基乙酰丙酸合成酶的激活剂,而氧合会导致这种三硫化物的细胞含量迅速下降。从有色素细胞中提取的胱硫醚酶(EC 4.2.1.15)可以催化由胱氨酸形成三硫化胱氨酸,而从相同细胞中提取的硫氰酸酶(EC 2.8.1.1)可以在亚硫酸盐存在的情况下催化三硫化胱氨酸降解形成胱氨酸和硫代硫酸盐。有人提出,三硫化胱氨酸的细胞含量是由胱硫醚酶以及可能还有硫氰酸酶的底物水平变化控制的,而不是由这些酶的量的变化控制。三硫化胱氨酸通过将该酶的低活性形式(b型)转化为高活性形式(a型)来控制氨基乙酰丙酸合成酶的活性。氧合时氨基乙酰丙酸合成酶活性的下降似乎是b型向a型转化停止以及a型向b型转化的结果。讨论了影响这些形式之间平衡的因素以及它们相互转化的可能机制。

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