The diversity of allosteric controls at the gateway to aromatic amino acid biosynthesis

Light, S.H.; Anderson, W.F.

doi:10.1002/pro.2233

Cited by 50 publications

(60 citation statements)

References 37 publications

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“…This endowed regulatory sensitivity to prephenate draws parallels to the DAH7PS from Bacillus subtilis, which is regulated by chorismate and prephenate via a covalently linked CM domain (32). The DAH7PS enzymes display a remarkably wide variety of allosteric mechanisms delivered by variable allosteric machinery appended to the core catalytic barrel (8). Of these, MtuDAH7PS appears to show the most sophisticated and elaborate allostery (9).…”

Section: Discussionmentioning

confidence: 97%

“…Because of its critical location at the start of the pathway, DAH7PS activity is usually tightly controlled by feedback regulation by pathway end products (8). M. tuberculosis DAH7PS * This work was supported in part by the Maurice Wilkins Centre for Biomolecular Discovery, by New Zealand Marsden Fund Grant UOC1105, and by a scholarship from the Maurice Wilkins Centre and the University of Canterbury (to N. J.…”

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confidence: 99%

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Complex Formation between Two Biosynthetic Enzymes Modifies the Allosteric Regulatory Properties of Both

Blackmore

Nazmi

Hutton

et al. 2015

Journal of Biological Chemistry

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Background: Two enzymes from Mycobacterium tuberculosis involved in aromatic amino acid biosynthesis form a heterooctameric complex. Results: Complex formation boosts the catalytic activity of both enzymes and greatly extends the allosteric effector sensitivity. Conclusion: Enzyme interactions allow complex allosteric machinery of one of the complex partners to be shared. Significance: Sophisticated allosteric responses are delivered through protein-protein interactions, allowing enhanced metabolic control.

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Section: Discussionmentioning

confidence: 97%

mentioning

confidence: 99%

Complex Formation between Two Biosynthetic Enzymes Modifies the Allosteric Regulatory Properties of Both

Blackmore

Nazmi

Hutton

et al. 2015

Journal of Biological Chemistry

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“…Various amino acids are produced in different biosynthetic pathways [60][61][62][63][64] (Figure 7). In few cases, some of the amino acids act as the substrate for the biosynthesis of other amino acids; whereas in other cases, allosteric inhibition of the biosynthesis of amino acids occurs [65][66][67]. In all of these amino acid biosynthetic pathways, along with substrate, ATP or NADH/NADPH are used as a source of energy.…”

Section: Leu Is a High-and Trp Is A Low-abundant Amino Acid In The Plmentioning

confidence: 99%

The Molecular Mass and Isoelectric Point of Plant Proteomes

Mohanta

Khan

Hashem

et al. 2019

Preprint

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Background Cell contain diverse array of proteins with different molecular weight and isoelectric point (pI). The molecular weight and pI of protein play important role in determining the molecular biochemical function. Therefore, it was important to understand the detail regarding the molecular weight and pI of the plant proteins. Results A proteome-wide analysis of plant proteomes from 145 species revealed a pI range of 1.99 (epsin) to 13.96 (hypothetical protein). The spectrum of molecular mass of the plant proteins varied from 0.54 to 2236.8 kDa. A putative Type-I polyketide synthase (22244 amino acids) in Volvox carteri was found to be the largest protein in the plant kingdom. However, Type-I polyketide synthase was not found in higher plant species. Titin (806.46 kDa) and misin/midasin (730.02 kDa) were the largest proteins identified in higher plant species. The pI and molecular weight of the plant proteins showed a trimodal distribution. An acidic pI (56.44% of proteins) was found to be predominant over a basic pI (43.34% of proteins) and the abundance of acidic pI proteins was higher in unicellular algae species relative to multicellular higher plants. In contrast, the seaweed, Porphyra umbilicalis, possesses a higher proportion of basic pI proteins (70.09%). Plant proteomes were also found to contain selenocysteine (Sec), amino acid that was found only in lower eukaryotic aquatic plant lineage. Amino acid composition analysis showed Leu was high and Trp was low abundant amino acids in the plant proteome. Additionally, the plant proteomes also possess ambiguous amino acids Xaa (unknown), Asx (asparagine or aspartic acid), Glx (glutamine or glutamic acid), and Xle (leucine or isoleucine) as well. Conclusion The diverse molecular weight and isoelectric point range of plant proteome will be helpful to understand their biochemical and functional aspects. The presence of selenocysteine proteins in lower eukaryotic organism is of interest and their expression in higher plant system can help us to understand their functional role.

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“…7). In few cases, some of the amino acids act as the substrate for the biosynthesis of other amino acids; whereas in other cases, allosteric inhibition of the biosynthesis of amino acids occurs [65][66][67]. In all of these amino acid biosynthetic pathways, along with substrate, ATP or NADH/NADPH are used as a source of energy.…”

Section: Leu Is a High-and Trp Is A Low-abundant Amino Acid In The Plmentioning

confidence: 99%

The Molecular Mass and Isoelectric Point of Plant Proteomes

Mohanta

Khan

Hashem

et al. 2019

Preprint

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12A proteomic analysis of proteomes from 145 plant species revealed a pI range of 1.99 (epsin) 13 to 13.96 (hypothetical protein). The molecular mass of the plant proteins ranged from 0.54 to 14 2236.8 kDa. A putative Type-I polyketide synthase (22244 amino acids) in Volvox carteri was 15 found to be the largest protein in the plant kingdom and was not found in higher plant species. 16 Titin (806.46 kDa) and misin/midasin (730.02 kDa) were the largest proteins identified in 17 higher plant species. The pI and molecular weight of the plant proteome exhibited a trimodal 18 distribution. An acidic pI (56.44% of proteins) was found to be predominant over a basic pI 19 (43.34% of proteins) and the abundance of acidic pI proteins was higher in unicellular algae 20 species relative to multicellular higher plants. In contrast, the seaweed, Porphyra umbilicalis, 21 possesses a higher proportion of basic pI proteins (70.09%). Plant proteomes were also found 22 to contain the amino acid, selenocysteine (Sec), which is the first report of the presence of this 23 amino acid in plants. Additionally, plant proteomes also possess ambiguous amino acids Xaa 24 (unknown), Asx (asparagine or aspartic acid), Glx (glutamine or glutamic acid), and Xle 25 (leucine or isoleucine) as well.26 27 Pyrrolysine 29 30 31 32 33The isoelectric or isoionic point of a protein is the pH at which a protein carries no net electrical 34 charge and hence is considered neutral 1-4 . The zwitterion form of a protein becomes dominant 35 at neutral pH. The pI of polypeptides is largely dependent on the dissociation constant of the 36 ionisable groups 5 . The major ionisable groups present in the amino acids are arginine, 37 aspartate, cysteine, histidine, glutamate, lysine, and glutamate, where they play a major role in 38 determining the pI of a protein 6-8 . Co-translational and post-translational modifications of a 39 protein, however, can also play a significant role in determining the pI of a protein 9,10 . The 40 exposure of charged residues to the solvents, hydrogen bonds (diploe interactions) and 41 dehydration also impact the pI of a protein 11,12 . The inherent pI of protein, however, is 42 primarily based on its native protein sequence. The pI of a protein is crucial to understanding 43 its biochemical function and thus determining pI is an essential aspect of proteomic studies. 44During electrophoresis, the direction of movement of a protein in a gel or other matrix depends 45 its'pI, hence numerous proteins can be separated based on their pI [13][14][15][16] . Given the impact of 46 post-translational modifications and other biochemical alterations (phosphorylation, 47 49 9,17,18. Nonetheless, an estimated isoelectric point is highly important and a commonly 50 identified parameter. 51Several studies have been conducted to understand the pI of proteins/polypeptides 3,19-21 . These 52 studies have been mainly based on animal, bacteria, and virus models and databases containing 53 the pI of experimentally verified proteins. None of these da...

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The diversity of allosteric controls at the gateway to aromatic amino acid biosynthesis

Cited by 50 publications

References 37 publications

Complex Formation between Two Biosynthetic Enzymes Modifies the Allosteric Regulatory Properties of Both

Complex Formation between Two Biosynthetic Enzymes Modifies the Allosteric Regulatory Properties of Both

The Molecular Mass and Isoelectric Point of Plant Proteomes

The Molecular Mass and Isoelectric Point of Plant Proteomes

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