Pages that link to "Q27652736"
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The following pages link to The 1.4 A crystal structure of the large and cold-active Vibrio sp. alkaline phosphatase (Q27652736):
Displaying 23 items.
- Coordination sphere of the third metal site is essential to the activity and metal selectivity of alkaline phosphatases (Q27658194) (← links)
- X-Ray Structure Reveals a New Class and Provides Insight into Evolution of Alkaline Phosphatases (Q27671653) (← links)
- Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes (Q28077585) (← links)
- Protein structure quality assessment based on the distance profiles of consecutive backbone Cα atoms. (Q30359279) (← links)
- The electrostatic profile of consecutive Cβ atoms applied to protein structure quality assessment. (Q30369767) (← links)
- Manipulation of enzyme properties by noncanonical amino acid incorporation (Q30454741) (← links)
- A novel cold-active and alkali-stable β-glucosidase gene isolated from the marine bacterium Martelella mediterranea (Q33587741) (← links)
- Cellular function and molecular structure of ecto-nucleotidases. (Q34031794) (← links)
- Active Site Detection by Spatial Conformity and Electrostatic Analysis—Unravelling a Proteolytic Function in Shrimp Alkaline Phosphatase (Q34103089) (← links)
- Structural phylogeny by profile extraction and multiple superimposition using electrostatic congruence as a discriminator (Q34418947) (← links)
- A measure of the broad substrate specificity of enzymes based on 'duplicate' catalytic residues (Q34482204) (← links)
- A novel bifunctional hybrid with marine bacterium alkaline phosphatase and Far Eastern holothurian mannan-binding lectin activities (Q34514377) (← links)
- A quantitative measure of electrostatic perturbation in holo and apo enzymes induced by structural changes (Q34630422) (← links)
- A computational module assembled from different protease family motifs identifies PI PLC from Bacillus cereus as a putative prolyl peptidase with a serine protease scaffold (Q34936357) (← links)
- LptO (PG0027) Is Required for Lipid A 1-Phosphatase Activity in Porphyromonas gingivalis W50. (Q36315627) (← links)
- Psychrophilic enzymes: from folding to function and biotechnology (Q37287783) (← links)
- Structural characteristics of alkaline phosphatase from the moderately halophilic bacterium Halomonas sp. 593. (Q37630128) (← links)
- Recombinant production and characterization of a highly active alkaline phosphatase from marine bacterium Cobetia marina (Q38303928) (← links)
- Zinc status and vacuolar zinc transporters control alkaline phosphatase accumulation and activity in Saccharomyces cerevisiae (Q42551925) (← links)
- The pH-dependent activation mechanism of Ser102 in Escherichia coli alkaline phosphatase: a theoretical study (Q47208023) (← links)
- Inhibition of a cold-active alkaline phosphatase by imipenem revealed by in silico modeling of metallo-β-lactamase active sites. (Q54327863) (← links)
- Marine enzymes and food industry: insight on existing and potential interactions (Q57899753) (← links)
- Chloride promotes refolding of active alkaline phosphatase through an inactive dimeric intermediate with an altered interface (Q60938105) (← links)