Substrate Binding and Catalysis in Carbamate Kinase Ascertained by Crystallographic and Site-Directed Mutagenesis Studies: Movements and Significance of a Unique Globular Subdomain of This Key Enzyme for Fermentative ATP Production in Bacteria

Ramón‐Maiques, Santiago; Marina, Alberto; Guinot, Anna; Gil-Ortiz, F.; Uriarte, Matxalen; Fita, Ignacio; Rubio, Vicente

doi:10.1016/j.jmb.2010.02.038

Cited by 21 publications

(38 citation statements)

References 31 publications

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“…3). In subunit B, the sulphate ion, a molecule that has been reported to occupy the position of the transferred phosphoryl groups 7,24 , also interacted with the main chain of the first turn of helix a5 (Fig. 3b), thus supporting the relevance of the a5 helix dipole in g-phosphate coordination.…”

Section: Resultsmentioning

confidence: 60%

Visualizing autophosphorylation in histidine kinases

2014

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Reversible protein phosphorylation is the most widespread regulatory mechanism in signal transduction. Autophosphorylation in a dimeric sensor histidine kinase is the first step in two-component signalling, the predominant signal-transduction device in bacteria. Despite being the most abundant sensor kinases in nature, the molecular bases of the histidine kinase autophosphorylation mechanism are still unknown. Furthermore, it has been demonstrated that autophosphorylation can occur in two directions, cis (intrasubunit) or trans (intersubunit) within the dimeric histidine kinase. Here, we present the crystal structure of the complete catalytic machinery of a chimeric histidine kinase. The structure shows an asymmetric histidine kinase dimer where one subunit is caught performing the autophosphorylation reaction. A structure-guided functional analysis on HK853 and EnvZ, two prototypical cis-and trans-phosphorylating histidine kinases, has allowed us to decipher the catalytic mechanism of histidine kinase autophosphorylation, which seems to be common independently of the reaction directionality.

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Section: Resultsmentioning

confidence: 60%

Visualizing autophosphorylation in histidine kinases

2014

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“…It also does not contain any gene for urea metabolism. Carbamate kinase, an unusual cyanobacterial enzyme involved in the production of ATP from ADP and carbamoyl phosphate in the final step of the fermentative degradation of arginine (32), is present in Cyanothece 7822, 8801, and 8802 and in Synechocystis 6803.…”

Section: Resultsmentioning

confidence: 99%

Novel Metabolic Attributes of the Genus Cyanothece , Comprising a Group of Unicellular Nitrogen-Fixing Cyanobacteria

Bandyopadhyay

Elvitigala

Welsh

et al. 2011

mBio

106

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The genus Cyanothece comprises unicellular cyanobacteria that are morphologically diverse and ecologically versatile. Studies over the last decade have established members of this genus to be important components of the marine ecosystem, contributing significantly to the nitrogen and carbon cycle. System-level studies of Cyanothece sp. ATCC 51142, a prototypic member of this group, revealed many interesting metabolic attributes. To identify the metabolic traits that define this class of cyanobacteria, five additional Cyanothece strains were sequenced to completion. The presence of a large, contiguous nitrogenase gene cluster and the ability to carry out aerobic nitrogen fixation distinguish Cyanothece as a genus of unicellular, aerobic nitrogen-fixing cyanobacteria. Cyanothece cells can create an anoxic intracellular environment at night, allowing oxygen-sensitive processes to take place in these oxygenic organisms. Large carbohydrate reserves accumulate in the cells during the day, ensuring sufficient energy for the processes that require the anoxic phase of the cells. Our study indicates that this genus maintains a plastic genome, incorporating new metabolic capabilities while simultaneously retaining archaic metabolic traits, a unique combination which provides the flexibility to adapt to various ecological and environmental conditions. Rearrangement of the nitrogenase cluster in Cyanothece sp. strain 7425 and the concomitant loss of its aerobic nitrogen-fixing ability suggest that a similar mechanism might have been at play in cyanobacterial strains that eventually lost their nitrogen-fixing ability.

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“…The final reactions of both ADI and AgDI pathways require CK with the end products ATP, CO 2 and NH 3 from carbamoylphosphate (Fig. 1e) (Ramó n-Maiques et al, 2010). For each mole of arginine or agmatine catabolized via the deiminase pathway, two moles of ammonia are produced.…”

Section: Discussionmentioning

confidence: 99%

Lmo0036, an ornithine and putrescine carbamoyltransferase in Listeria monocytogenes, participates in arginine deiminase and agmatine deiminase pathways and mediates acid tolerance

et al. 2011

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Listeria monocytogenes is a foodborne pathogen causing listeriosis. Acid is one of the stresses that foodborne pathogens encounter most frequently. The ability to survive and proliferate in acidic environments is a prerequisite for infection. However, there is limited knowledge about the molecular basis of adaptation of L. monocytogenes to acid. Arginine deiminase (ADI) and agmatine deiminase (AgDI) systems are implicated in bacterial tolerance to acidic environments. Homologues of ADI and AgDI systems have been found in L. monocytogenes lineages I and II strains. Sequence analysis indicated that lmo0036 encodes a putative carbamoyltransferase containing conserved motifs and residues important for substrate binding. Lmo0036 acted as an ornithine carbamoyltransferase and putrescine carbamoyltransferase, representing the first example, to our knowledge, that catalyses reversible ornithine and putrescine carbamoyltransfer reactions. Catabolic ornithine and putrescine carbamoyltransfer reactions constitute the second step of ADI and AgDI pathways. However, the equilibrium of in vitro carbamoyltransfer reactions was overwhelmingly towards the anabolic direction, suggesting that catabolic carbamoyltransferase was probably the limiting step of the pathways. lmo0036 was induced at the transcriptional level when L. monocytogenes was subjected to low-pH stress. Its expression product in Escherichia coli exhibited higher catabolic carbamoyltransfer activities under acidic conditions. Consistently, absence of this enzyme impaired the growth of Listeria under mild acidic conditions (pH 4.8) and reduced its survival in synthetic human gastric fluid (pH 2.5), and corresponded to a loss in ammonia production, indicating that Lmo0036 was responsible for acid tolerance at both sublethal and lethal pH levels. Furthermore, Lmo0036 played a possible role in Listeria virulence.

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Substrate Binding and Catalysis in Carbamate Kinase Ascertained by Crystallographic and Site-Directed Mutagenesis Studies: Movements and Significance of a Unique Globular Subdomain of This Key Enzyme for Fermentative ATP Production in Bacteria

Cited by 21 publications

References 31 publications

Visualizing autophosphorylation in histidine kinases

Visualizing autophosphorylation in histidine kinases

Novel Metabolic Attributes of the Genus Cyanothece , Comprising a Group of Unicellular Nitrogen-Fixing Cyanobacteria

Lmo0036, an ornithine and putrescine carbamoyltransferase in Listeria monocytogenes, participates in arginine deiminase and agmatine deiminase pathways and mediates acid tolerance

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