The interconversion of ACC deaminase and d-cysteine desulfhydrase by directed mutagenesis

Todorović, Biljana; Glick, Bernard R.

doi:10.1007/s00425-008-0820-3

Cited by 72 publications

(52 citation statements)

References 60 publications

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“…Moreover, all putative AcdS sequences were analyzed for key protein residues known to be important for ACC deaminase activity, namely Lys51, Ser78, Tyr295, Glu296 and Leu322 [7], [57], [58] using Pseudomonas sp. UW4 as a reference.…”

Section: Methodsmentioning

confidence: 99%

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New Insights into 1-Aminocyclopropane-1-Carboxylate (ACC) Deaminase Phylogeny, Evolution and Ecological Significance

et al. 2014

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The main objective of this work is the study of the phylogeny, evolution and ecological importance of the enzyme 1-aminocyclopropane-1-carboxylate (ACC) deaminase, the activity of which represents one of the most important and studied mechanisms used by plant growth–promoting microorganisms. The ACC deaminase gene and its regulatory elements presence in completely sequenced organisms was verified by multiple searches in diverse databases, and based on the data obtained a comprehensive analysis was conducted. Strain habitat, origin and ACC deaminase activity were taken into account when analyzing the results. In order to unveil ACC deaminase origin, evolution and relationships with other closely related pyridoxal phosphate (PLP) dependent enzymes a phylogenetic analysis was also performed. The data obtained show that ACC deaminase is mostly prevalent in some Bacteria, Fungi and members of Stramenopiles. Contrary to previous reports, we show that ACC deaminase genes are predominantly vertically inherited in various bacterial and fungal classes. Still, results suggest a considerable degree of horizontal gene transfer events, including interkingdom transfer events. A model for ACC deaminase origin and evolution is also proposed. This study also confirms the previous reports suggesting that the Lrp-like regulatory protein AcdR is a common mechanism regulating ACC deaminase expression in Proteobacteria, however, we also show that other regulatory mechanisms may be present in some Proteobacteria and other bacterial phyla. In this study we provide a more complete view of the role for ACC deaminase than was previously available. The results show that ACC deaminase may not only be related to plant growth promotion abilities, but may also play multiple roles in microorganism's developmental processes. Hence, exploring the origin and functioning of this enzyme may be the key in a variety of important agricultural and biotechnological applications.

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Section: Methodsmentioning

confidence: 99%

“…The AcdS sequences were aligned using MUSCLE [59] and the presence of key amino acid positions were verified. Sequences presenting different amino acids in the above mentioned positions were discarded, as they are likely to represent related PLP dependent enzymes, such as D-cysteine desulfhydrase [58].…”

Section: Methodsmentioning

confidence: 99%

New Insights into 1-Aminocyclopropane-1-Carboxylate (ACC) Deaminase Phylogeny, Evolution and Ecological Significance

et al. 2014

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“…l-Cysteine-glutathione disulfide, but not the d-cysteine analog, protected mice against acetaminophen-induced liver damage [160]. d-Cysteine desulfhydrase catalyzes the elimination of H 2 S form d-cysteine, presumably to form dehydroalanine [161].…”

Section: 4mentioning

confidence: 99%

Origin, Microbiology, Nutrition, and Pharmacology of D‐Amino Acids

Friedman

2010

Chemistry & Biodiversity

162

108

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Exposure of food proteins to certain processing conditions induces two major chemical changes: racemization of all L-amino acids (LAAs) to D-amino acids (DAAs) and concurrent formation of cross-linked amino acids such as lysinoalanine (LAL). The diet contains both processing-induced and naturally-formed DAA. The latter include those found in microorganisms, plants, and marine invertebrates. Racemization impairs digestibility and nutritional quality. Racemization of LAA residues to their D-isomers in food and other proteins is pH-, time-, and temperature-dependent. Although racemization rates of LAA residues in a protein vary, relative rates in different proteins are similar. The nutritional utilization of different DAAs varies widely in animals and humans. Some DAAs may exert both adverse and beneficial biological effects. Thus, although D-Phe is utilized as a nutritional source of L-Phe, high concentrations of D-Tyr in such diets inhibit the growth of mice. Both D-Ser and LAL induce histological changes in the rat kidney. The wide variation in the utilization of DAAs is illustrated by the fact that, whereas D-Meth is largely utilized as a nutritional source of the L-isomer, D-Lys is not. Similarly, although L-CysSH has a sparing effect on L-Meth when fed to mice, D-CysSH does not. Since DAAs are consumed as part of their normal diet, a need exists to develop a better understanding of their roles in foods, microbiology, nutrition, and medicine. To contribute to this effort, this overview surveys our present knowledge of the chemistry, nutrition, safety, microbiology, and pharmacology of DAAs. Also covered are the origin and distribution of DAAs in food and possible roles of DAAs in human physiology, aging, and the etiology and therapy of human diseases.

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“…In fact, it has been demonstrated that the two enzymes can be interconverted by altering only two amino acid residues (Todorovic and Glick 2008 ). However, D -cysteine desulfhydrase uses D -cysteine as a substrate rather than ACC.…”

Section: Probes To Pcr Amplify Acc Deaminase Genesmentioning

confidence: 99%

Methods to Study 1-Aminocyclopropane-1-carboxylate (ACC) Deaminase in Plant Growth-Promoting Bacteria

Brı́gido

Duan

Glick

2015

Handbook for Azospirillum

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The lowering of plant ethylene levels by the enzyme 1-aminocyclopropane-1-carboxylate (ACC) deaminase is one of the key mechanisms employed by plant growth-promoting bacteria (PGPB) to facilitate plant growth. Since its discovery, it has been detected in both fungi and bacteria. It has been shown by a large number of workers in a wide range of bacteria that the activity of this enzyme in PGPB is important during normal plant development and also protects plants from the deleterious effects of a wide range of environmental stresses. ACC deaminase-containing PGPB bound to a plant act as a sink for ACC, thereby lowering ethylene levels in plant tissues. The result of the functioning of this enzyme is an increase in the growth of plant roots and shoots and a reduction of the inhibitory effects of ethylene synthesis especially during stressful conditions. This chapter briefl y summarizes the current knowledge of various ACC deaminases emphasizing the use of ACC deaminase-containing bacteria in promoting plant growth under diverse biotic and abiotic stresses, and describes methods for the isolation and study of ACC deaminase-containing bacteria.

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The interconversion of ACC deaminase and d-cysteine desulfhydrase by directed mutagenesis

Cited by 72 publications

References 60 publications

New Insights into 1-Aminocyclopropane-1-Carboxylate (ACC) Deaminase Phylogeny, Evolution and Ecological Significance

New Insights into 1-Aminocyclopropane-1-Carboxylate (ACC) Deaminase Phylogeny, Evolution and Ecological Significance

Origin, Microbiology, Nutrition, and Pharmacology of D‐Amino Acids

Methods to Study 1-Aminocyclopropane-1-carboxylate (ACC) Deaminase in Plant Growth-Promoting Bacteria

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