Occurrence, functions and biosynthesis of polyamides in microorganisms and biotechnological production

Oppermann‐Sanio, Fred Bernd; Steinbüchel, Alexander

doi:10.1007/s00114-001-0280-0

Cited by 187 publications

(126 citation statements)

References 127 publications

(130 reference statements)

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“…It comprises a polyaspartate backbone with arginine side chains attached via their a-amino group to the b-carboxy group of each aspartate ( Figure 3). It is synthesized by cyanophycin synthetase without the involvement of ribosomes, and deposited as granules (Berg et al, 2000;Oppermann-Sanio and Steinbü -chel, 2002). Although cyanophycin is not a polymer with good material properties, it is of interest mainly as a source of polyaspartate, which could replace the chemically synthesized material used as a super-adsorbant or anti-scalant (Oppermann-Sanio and Steinbü chel, 2002).…”

Section: Non-ribosomally Produced Poly-amino Acidsmentioning

confidence: 99%

Production of renewable polymers from crop plants

Beilen

Poirier²

2008

The Plant Journal

142

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SummaryPlants produce a range of biopolymers for purposes such as maintenance of structural integrity, carbon storage, and defense against pathogens and desiccation. Several of these natural polymers are used by humans as food and materials, and increasingly as an energy carrier. In this review, we focus on plant biopolymers that are used as materials in bulk applications, such as plastics and elastomers, in the context of depleting resources and climate change, and consider technical and scientific bottlenecks in the production of novel or improved materials in transgenic or alternative crop plants. The biopolymers discussed are natural rubber and several polymers that are not naturally produced in plants, such as polyhydroxyalkanoates, fibrous proteins and poly-amino acids. In addition, monomers or precursors for the chemical synthesis of biopolymers, such as 4-hydroxybenzoate, itaconic acid, fructose and sorbitol, are discussed briefly.

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Section: Non-ribosomally Produced Poly-amino Acidsmentioning

confidence: 99%

Production of renewable polymers from crop plants

Beilen

Poirier²

2008

The Plant Journal

142

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“…1). The 857-901-amino acid CphA proteins, found mostly in cyanobacterial backgrounds, catalyze the ATP-dependent synthesis of the storage polymer multi-L-arginylpoly-L-aspartic acid (cyanophycin), thereby sequentially adding an aspartic acid residue and an arginine residue to a ␤-Asp-Arg primer (38). These two ATP-dependent carboxyl-to-amine ligase reactions take place in the active sites of two distinct domains: a C-terminal domain, starting approximately just before the second half of the sequence, which falls into a superfamily of Rossman fold-containing peptide ligases including certain murein ligases and folyl poly-␥-glutamate ligase; and an N-terminal domain that groups within the ATPgrasp superfamily of ATP-dependent ligases (20).…”

Section: Probing Glutathione Biosynthesis Among Pasteurellaceae By Idmentioning

confidence: 99%

Characterization of the Bifunctional γ-Glutamate-cysteine Ligase/Glutathione Synthetase (GshF) of Pasteurella multocida

Vergauwen

Vos

Beeumen

2006

Journal of Biological Chemistry

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Glutamate-cysteine ligase (␥-ECL) and glutathione synthetase (GS) are the two unrelated ligases that constitute the glutathione biosynthesis pathway in most eukaryotes, purple bacteria, and cyanobacteria. ␥-ECL is a member of the glutamine synthetase family, whereas GS enzymes group together with highly diverse carboxylto-amine/thiol ligases, all characterized by the so-called two-domain ATP-grasp fold. This generalized scheme toward the formation of glutathione, however, is incomplete, as functional steadystate levels of intracellular glutathione may also accumulate solely by import, as has been reported for the Pasteurellaceae member Haemophilus influenzae, as well as for certain Gram-positive enterococci and streptococci, or by the action of a bifunctional fusion protein (termed GshF), as has been reported recently for the Gram-positive firmicutes Streptococcus agalactiae and Listeria monocytogenes. Here, we show that yet another member of the Pasteurellaceae family, Pasteurella multocida, acquires glutathione both by import and GshF-driven biosynthesis. Domain architecture analysis shows that this P. multocida GshF bifunctional ligase contains an N-terminal ␥-proteobacterial ␥-ECL-like domain followed by a typical ATP-grasp domain, which most closely resembles that of cyanophycin synthetases, although it has no significant homology with known GS ligases. Recombinant P. multocida GshF overexpresses as an ϳ85-kDa protein, which, on the basis of gel-sizing chromatography, forms dimers in solution. The ␥-ECL activity of GshF is regulated by an allosteric type of glutathione feedback inhibition (K i ‫؍‬ 13.6 mM). Furthermore, steady-state kinetics, on the basis of which we present a novel variant of half-of-the-sites reactivity, indicate intimate domain-domain interactions, which may explain the bifunctionality of GshF proteins.Glutathione (GSH; L-␥-glutamyl-L-cysteinylglycine) is the predominant low molecular weight peptide thiol present in many Gram-negative bacteria and in virtually all eukaryotes, except those that lack mitochondria (1, 2). Glutathione is made in a highly conserved two-step ATP-dependent biosynthesis pathway by two unrelated peptide bondforming enzymes (3). In the first and rate-limiting reaction, ␥-glutamate-cysteine ligase (␥-ECL) 2 (EC 6.3.2.2) condenses the ␥-carboxylate of L-glutamic acid with L-cysteine to form the dipeptide ␥-glutamylcys-where Me 2ϩ can be magnesium or manganese (4, 5). In the second step, ␥-EC is condensed with glycine in a reaction catalyzed by glutathione synthetase (GS; EC 6.3.2.3), according towhere Me 2ϩ again can be magnesium or manganese. The activity of eukaryotic ␥-ECL is precisely controlled by nonallosteric glutathione feedback inhibition, the limited availability of cellular L-Cys, and the transcriptional and posttranslational regulation of the expression and activity of the enzyme under various physiological conditions (6). Bacterial glutathione homeostasis is less well characterized, although glutathione feedback inhibition appears to be of major importa...

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“…7 and cited references therein), only a few reports are available on the intracellular degradation of CGP. Intracellular CGP degradation was first observed in crude extracts of soluble proteins prepared from cells of Anabaena cylindrica (5).…”

mentioning

confidence: 99%

Isolation of Cyanophycin-degrading Bacteria, Cloning and Characterization of an Extracellular Cyanophycinase Gene (cphE) from Pseudomonas anguilliseptica Strain BI

Obst¹,

Oppermann‐Sanio²,

Luftmann³

et al. 2002

Journal of Biological Chemistry

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Eleven bacteria capable of utilizing cyanophycin (cyanophycin granule polypeptide (CGP)) as a carbon source for growth were isolated. One isolate was taxonomically affiliated as Pseudomonas anguilliseptica strain BI, and the extracellular cyanophycinase (CphE) was studied because utilization of cyanophycin as a carbon source and extracellular cyanophycinases were hitherto not described. CphE was detected in supernatants of CGP cultures and purified from a corresponding culture of strain BI employing chromatography on the anion exchange matrix Q-Sepharose and on an arginineagarose affinity matrix. The mature form of the inducible enzyme consisted of one type of subunit with M r ‫؍‬ 43,000 and exhibited high specificity for CGP, whereas proteins and synthetic polyaspartic acid were not hydrolyzed or were only marginally hydrolyzed. Degradation products of the enzyme reaction were identified as aspartic acid-arginine dipeptides (␤-Asp-Arg) by high performance liquid chromatography and electrospray ionization mass spectrometry. The corresponding gene (cphE, 1254 base pairs) was identified in subclones of a cosmid gene library of strain BI by heterologous active expression in Escherichia coli, and its nucleotide sequence was determined. The enzyme exhibited only 27-28% amino acid sequence identity to intracellular cyanophycinases occurring in cyanobacteria. Analysis of the amino acid sequence of cphE revealed a putative catalytic triad consisting of the motif GXSXG plus a histidine and most probably a glutamate residue. In addition, the strong inhibition of the enzyme by Pefabloc ® and phenylmethylsulfonyl fluoride indicated that the catalytic mechanism of CphE is related to that of serine type proteases. Quantitative analysis on the release of ␤-Asp-Arg dipeptides from C-terminal labeled CGP gave evidence for an exo-degradation mechanism.Cyanophycin (cyanophycin granule polypeptide, CGP) 1 is a naturally occurring poly(amino acid), which is synthesized in most cyanobacteria as nitrogen, carbon, and energy storage compound in the early stationary growth phase (1, 2). The water-insoluble CGP is accumulated intracellularly in the form of membraneless granules (3) and is degraded by the cells when growth is resumed. The backbone of this unique biopolymer consists of ␣-amino-␣-carboxyl-linked L-aspartic acid monomers. Most of the ␤-carboxylic groups are covalently bound to the ␣-amino groups of L-arginine residues (4, 5); in recombinant Escherichia coli expressing cyanobacterial CGP-synthesizing enzymes (see below), a significant fraction of arginine is replaced by lysine (6).Although much information has been obtained concerning the non-ribosomal biosynthesis of CGP, which is catalyzed by the cyanophycin synthetase (CphA; see Ref. 7 and cited references therein), only a few reports are available on the intracellular degradation of CGP. Intracellular CGP degradation was first observed in crude extracts of soluble proteins prepared from cells of Anabaena cylindrica (5). The corresponding enzyme, cyanophycinase (CphB), was...

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Occurrence, functions and biosynthesis of polyamides in microorganisms and biotechnological production

Cited by 187 publications

References 127 publications

Production of renewable polymers from crop plants

Production of renewable polymers from crop plants

Characterization of the Bifunctional γ-Glutamate-cysteine Ligase/Glutathione Synthetase (GshF) of Pasteurella multocida

Isolation of Cyanophycin-degrading Bacteria, Cloning and Characterization of an Extracellular Cyanophycinase Gene (cphE) from Pseudomonas anguilliseptica Strain BI

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