The 1.4 Å crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase

Helland, Ronny; Larsen, Renate Lie; Ásgeirsson, Bjarni

doi:10.1016/j.bbapap.2008.09.020

Cited by 51 publications

(68 citation statements)

References 59 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…A crown domain is also present in the APs from Halobacterium salinarum [591] and Vibrio sp. [592], but it has a different fold in the bacterial enzymes. (3) Finally, a metal-binding domain consisting of 76 residues (209-285) is present at the distal ends of the longest axis of the dimer.…”

Section: Phylogenetic Relationshipmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

871

922

View full text Add to dashboard Cite

Ecto-nucleotidases play a pivotal role in purinergic signal transmission. They hydrolyze extracellular nucleotides and thus can control their availability at purinergic P2 receptors. They generate extracellular nucleosides for cellular reuptake and salvage via nucleoside transporters of the plasma membrane. The extracellular adenosine formed acts as an agonist of purinergic P1 receptors. They also can produce and hydrolyze extracellular inorganic pyrophosphate that is of major relevance in the control of bone mineralization. This review discusses and compares four major groups of ectonucleotidases: the ecto-nucleoside triphosphate diphosphohydrolases, ecto-5′-nucleotidase, ecto-nucleotide pyrophosphatase/phosphodiesterases, and alkaline phosphatases. Only recently and based on crystal structures, detailed information regarding the spatial structures and catalytic mechanisms has become available for members of these four ecto-nucleotidase families. This permits detailed predictions of their catalytic mechanisms and a comparison between the individual enzyme groups. The review focuses on the principal biochemical, cell biological, catalytic, and structural properties of the enzymes and provides brief reference to tissue distribution, and physiological and pathophysiological functions.

show abstract

Section: Phylogenetic Relationshipmentioning

confidence: 99%

Cellular function and molecular structure of ecto-nucleotidases

Zimmermann

Zebisch

Sträter

2012

Purinergic Signalling

871

922

View full text Add to dashboard Cite

show abstract

“…Based on the crystal structure of Aspergillus flavus uricase, which is homologous to C. utilis uricase, two Phe residues, Phe170 and Phe281, were chosen as non-essential residues to comprise the active site of uricase. Although the uricase variant containing (35) at either Phe170 or Phe281 exhibited reduced activity by 50 or 78%, respectively, these results demonstrated the feasibility of incorporating a reactive aryl azide functional group into a target enzyme for site-specific glycosylation and PEGylation [87].…”

Section: Improvement Of Enzyme Activity and Stability By Site-specifimentioning

confidence: 85%

“…Alternatively, Chin et al [92,93] developed an orthogonal ribosome, which efficiently decoded a series of four-base codons and an amber codon, and combined the orthogonal ribosome with mutually orthogonal aaRS/tRNA pairs to achieve incorporation of two different NCAAs into a single protein in vivo. As a model system, Chin et al [93] introduced both (35) and L-N-6-[(2-proplynyloxy)carbonyl]lysine into a GST-calmodulin fusion protein in response to AGGA and amber codons, respectively. These findings also suggested that the orthogonal aaRS/tRNA pairs already developed could be modified to achieve multiple NCAA incorporation in vivo.…”

Section: Discussionmentioning

confidence: 99%

“…Replacing multiple histidine residues in alkaline phosphate with histidine analogues, 1,2,4-triazole-3-alanine (1) or 2-methylhistidine (2), leads to failure of native dimer formation or complete loss in activity, respectively [32,33]. Structural studies on alkaline phosphatases revealed that histidine residues played a pivotal role in maintaining metal ions in active sites [31,34,35]. Therefore, the perturbed folded structure and activity of alkaline phosphatase can be attributed to modifying the enzyme active center by replacing histidine residues with histidine analogues.…”

Section: Residue-specific Incorporation Of Ncaas Into Enzymesmentioning

confidence: 99%

See 1 more Smart Citation

Manipulation of enzyme properties by noncanonical amino acid incorporation

Zheng

Kwon

2011

Biotechnology Journal

View full text Add to dashboard Cite

Since wild-type enzymes do not always have the properties needed for various applications, enzymes are often engineered to obtain desirable properties through protein engineering techniques. In the past decade, complementary to the widely used rational protein design and directed evolution techniques, noncanonical amino acid incorporation (NCAAI) has become a new and effective protein engineering technique. Recently, NCAAI has been used to improve intrinsic functions of proteins, such as enzymes and fluorescent proteins, beyond the capacities obtained with natural amino acids. Herein, recent progress on improving enzyme properties through NCAAI in vivo is reviewed and the challenges of current approaches and future directions are also discussed. To date, both NCAAI methods-residue- and site-specific incorporation-have been primarily used to improve the catalytic turnover number and substrate binding affinity of enzymes. Numerous strategies used to minimize structural perturbation and stability loss of a target enzyme upon NCAAI are also explored. Considering the generality of NCAAI incorporation, we expect its application could be expanded to improve other enzyme properties, such as substrate specificity and solvent resistance in the near future.

show abstract

“…The cold active nature was assigned to the combination of a significant random coil presence (46%) which makes the molecular structure highly flexible, a pattern enhanced by the presence of aspartic acid, valine, serine, glycine, and alanine around the active site, together with a ratio of asparagines and glycines to arginines and prolines of 1.42 (Mao et al, 2010). These features have been related to the ability of enzymes to adapt to low temperatures (Huston et al, 2004;Bauvois et al, 2008;Helland et al, 2009). This pattern is thus associated with the high flexibility of psycrophilic enzymes, which involves a decrease in weak interactions or the fading of stability factors, leading to improved dynamics of active site residues under low temperatures (Struvay and Feller, 2012).…”

Section: Glucosidasesmentioning

confidence: 99%

Marine enzymes and food industry: insight on existing and potential interactions

Fernandes

2014

Front. Mar. Sci.

View full text Add to dashboard Cite

Evidence that support the marine environment as source of useful biocatalysts for application in several areas of industry pile up, both as scientific reports or patent applications. Marine microorganisms have to endure habitats characterized by extreme conditions of salinity, temperature or pressure. Their enzymes present concomitant features, viz. thermostability or halostability, which are appealing for practical applications. The food sector is a field where enzymes are used, given their specificity, compliance with strict regulations, relatively mild operational conditions required and environmental friendly nature. The specific features presented by marine enzymes can be advantageously used both for process improvement or to develop new processes and products. In the present review the role of relevant types of enzymes for the food sector is described and recent findings on those enzymes from marine are put into context. The information provided is illustrative that in spite of the relative novelty concerning the use of marine enzymes within the scope of the food sector, some processes have reached commercial status and promising results are being obtained with several others. Moreover, there is still a vast field of resources for enzyme activity to be explored, namely since the screening process that has been considerably improved with the contribution of metagenomic libraries. It can thus be considered that future and exciting developments can be expected concerning the use of marine enzymes in the food and feed areas.

show abstract

The 1.4 Å crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase

Cited by 51 publications

References 59 publications

Cellular function and molecular structure of ecto-nucleotidases

Cellular function and molecular structure of ecto-nucleotidases

Manipulation of enzyme properties by noncanonical amino acid incorporation

Marine enzymes and food industry: insight on existing and potential interactions

Contact Info

Product

Resources

About