Heat-labile bacterial alkaline phosphatase from a marine Vibrio sp.

Hauksson, Jónas B.; Andrésson, Ólafur S.; Ásgeirsson, Bjarni

doi:10.1016/s0141-0229(00)00152-6

Cited by 58 publications

(34 citation statements)

References 53 publications

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“…These enzymes appear to be distinct from their terrestrial counterparts in substrate preference, metal binding ligands, P i affinity, thermostability, and catalytic efficiency. The marine bacterial APs such as the Antarctic psychrophile TAB5 (Rina et al 2000), the psychrophile Vibrio G15-21 (Hauksson et al 2000), the psychrophiles Shewanella sp. (Murakawa et al 2002) and Shewanella sp.…”

Section: Discussionmentioning

confidence: 99%

“…The kinetic parameters of CmAP were 0.3-13.2 mM (K m ) and 24,000-28,300 s (k cat ) with the catalytic efficiency of 2.1× 10 6 -8.2×10 7 s/M (Table 2). For comparison, the K m of E. coli AP was 0.06 mM and a k cat of 62 s with the catalytic efficiency of 1.1×10 6 , whereas the K m of bovine intestinal AP, including its catalytically improved mutants, ranged from 1.3 to 3.9 mM and the k cat ranged from 1,800 to 6,100 s with the catalytic efficiency of 1.4-1.6 × 10 6 s/M (Hauksson et al 2000;Kozlenkov et al 2002). Surprisingly, the native C. marina AP signal peptide was found to be appropriate for E. coli system to produce periplasmic recombinant protein (Nasu et al 2012).…”

Section: Discussionmentioning

confidence: 99%

“…6). (Hauksson et al 2000;Helland et al 2009). A relatively lower identity (≤38 %) and similarity (≤52 %) were observed for other APs, including AP from Antarctic bacterium TAB5 and mammalian and marine invertebrate APs (Rina et al 2000;Le Du et al 2001;De Backer et al 2002;Kozlenkov et al 2002).…”

Section: Effects Of Chemicals On Cmapmentioning

confidence: 99%

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Recombinant Production and Characterization of a Highly Active Alkaline Phosphatase from Marine Bacterium Cobetia marina

et al. 2014

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The psychrophilic marine bacterium, Cobetia marina, recovered from the mantle tissue of the marine mussel, Crenomytilus grayanus, which contained a gene encoding alkaline phosphatase (AP) with apparent biotechnology advantages. The enzyme was found to be more efficient than its counterparts and showed k cat value 10-to 100-fold higher than those of all known commercial APs. The enzyme did not require the presence of exogenous divalent cations and dimeric state of its molecule for activity. The recombinant enzyme (CmAP) production and purification were optimized with a final recovery of 2 mg of the homogenous protein from 1 L of the transgenic Escherichia coli Rosetta(DE3)/Pho40 cells culture. CmAP displayed a half-life of 16 min at 45°C and 27 min at 40°C in the presence of 2 mM EDTA, thus suggesting its relative thermostability in comparison with the known cold-adapted analogues. A high concentration of EDTA in the incubation mixture did not appreciably inhibit CmAP. The enzyme was stable in a wide range of pH (6.0-11.0). CmAP exhibited its highest activity at the reaction temperature of 40-50°C and pH 9.5-10.3. The structural features of CmAP could be the reason for the increase in its stability and catalytic turnover. We have modeled the CmAP 3D structure on the base of the high-quality experimental structure of the close homologue Vibrio sp. AP (VAP) and mutated essential residues predicted to break Mg 2+ bonds in CmAP. It seems probable that the intrinsically tight binding of catalytic and structural metal ions together with the flexibility of intermolecular and intramolecular links in CmAP could be attributed to the adapted mutualistic lifestyle in oceanic waters.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Recombinant Production and Characterization of a Highly Active Alkaline Phosphatase from Marine Bacterium Cobetia marina

et al. 2014

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“…APs are classically described as being homodimeric, which is the case with E. coli and mammalian APs. However, many monomeric (13,19,40) and oligomeric (17) forms have been described. Further studies may provide clarification of the parameters governing the equilibrium between the two forms.…”

Section: Discussionmentioning

confidence: 99%

Characterization of a Highly Thermostable Alkaline Phosphatase from the EuryarchaeonPyrococcus abyssi

Zappa

Rolland

Flament

et al. 2001

Appl Environ Microbiol

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This work reports the first isolation and characterization of an alkaline phosphatase (AP) from a hyperthermophilic archaeon. An AP gene from Pyrococcus abyssi, a euryarchaeon isolated from a deep-sea hydrothermal vent, was cloned and the enzyme expressed in Escherichia coli. Analysis of the sequence showed conservation of the active site and structural elements of the E. coli AP. The recombinant AP was purified and characterized. Monomeric and homodimeric active forms were detected, with a monomer molecular mass of 54 kDa. Apparent optimum pH and temperature were estimated at 11.0 and 70°C, respectively. Thus far, P. abyssi AP has been demonstrated to be the most thermostable AP, with half-lives at 100 and 105°C of 18 and 5 h, respectively. Enzyme activity was found to be dependent on divalent cations: metal ion chelators inhibited activity, whereas the addition of exogenous Mg(II), Zn(II), and Co(II) increased activity. The enzyme was inhibited by inorganic phosphate, but not by molybdate and vanadate. Strong inhibitory effects were observed in the presence of thiolreducing agents, although cysteine residues of the P. abyssi AP were not found to be incorporated within intraor interchain disulfide bonds. In addition, P. abyssi AP was demonstrated to dephosphorylate linear DNA fragments with dephosphorylation efficiencies of 93.8 and 84.1% with regard to cohesive and blunt ends, respectively.

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“…Hauksson [23] have described phosphatase producing marine vibrio sp. Bacteria associated with the marine sponge Haliclona sp have also been reported producing phosphatase enzyme [24].…”

Section: Discussionmentioning

confidence: 99%

Sponge-associated bacteria of Lakshadweep coral reefs, India: resource for extracellular hydrolytic enzymes

Feby¹,

Nair²

2010

ABB

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Sponges (Phylum: Porifera) is one of the major groups in the Lakshadweep coral reefs. These sponges harbor diverse bacteria with metabolic potentiality. From biodiversity to biotechnological prospecting, scientific investigations related to sponge associated microorganisms have expanded, but remain rather limited to few geographic locations. In this study, culturable bacteria associated with two demosponges viz Dysidea granulosa, Sigmadocia fibulata and the ambient water were screened for commercially important enzymes such as amylase, protease, gelatinase, lipase, deoxyribonucleic, phosphatase and urease. Amylase and phosphatase were the predominant enzymes produced by >80% of sponge-associated bacteria compared to the ambient water. Nearly 50% of the sponge-associated bacteria expressed multiple enzymatic activities (> 4) with variation in the percentage of expression of individual enzymes. More than 65% of the culturable heterotrophic bacteria associated with sponges were Gammaproteobacteria. The order Vibrionales was the main source for multiple enzyme production. Sponge associated bacteria formed more closely related clusters than the water isolates based upon their activity pattern. High recovery of sponge-associated bacteria with multiple enzymatic activities suggest that these versatile bacteria are yet unexploited potential for bioprospecting.

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Heat-labile bacterial alkaline phosphatase from a marine Vibrio sp.

Cited by 58 publications

References 53 publications

Recombinant Production and Characterization of a Highly Active Alkaline Phosphatase from Marine Bacterium Cobetia marina

Recombinant Production and Characterization of a Highly Active Alkaline Phosphatase from Marine Bacterium Cobetia marina

Characterization of a Highly Thermostable Alkaline Phosphatase from the EuryarchaeonPyrococcus abyssi

Sponge-associated bacteria of Lakshadweep coral reefs, India: resource for extracellular hydrolytic enzymes

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