15 research outputs found
Integration of TTF, UTAUT, and ITM for mobile Banking Adoption
The introduction of mobile banking facility has enabled customers to carry out banking transactionswith the use of smartphones and other handheld devices from anywhere. It has become a luxurious and exclusive method of online payments. The recent growth of telecommunication sector and a tremendous increase in mobile USAge has opened new doors for sparking future of banking sector industry. The following research is aimed to find out the mobile banking adoption attitudes with the integration of TTF, UTAUT,and ITM models
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Structural and Functional Characterization of MppR, an Enduracididine Biosynthetic Enzyme from Streptomyces hygroscopicus: Functional Diversity in the Acetoacetate Decarboxylase-like Superfamily
The nonproteinogenic amino acid enduracididine is a critical component of the mannopeptimycins, cyclic glycopeptide antibiotics with activity against drug-resistant pathogens, including methicillin-resistant Staphylococcus aureus. Enduracididine is produced in Streptomyces hygroscopicus by three enzymes, MppP, MppQ, and MppR. On the basis of primary sequence analysis, MppP and MppQ are pyridoxal 5'-phosphate-dependent aminotransferases; MppR shares a low, but significant, level of sequence identity with acetoacetate decarboxylase. The exact reactions catalyzed by each enzyme and the intermediates involved in the route to enduracididine are currently unknown. Herein, we present biochemical and structural characterization of MppR that demonstrates a catalytic activity for this enzyme and provides clues about its role in enduracididine biosynthesis. Bioinformatic analysis shows that MppR belongs to a previously uncharacterized family within the acetoacetate decarboxylase-like superfamily (ADCSF) and suggests that MppR-like enzymes may catalyze reactions diverging from the well-characterized, prototypical ADCSF decarboxylase activity. MppR shares a high degree of structural similarity with acetoacetate decarboxylase, though the respective quaternary structures differ markedly and structural differences in the active site explain the observed loss of decarboxylase activity. The crystal structure of MppR in the presence of a mixture of pyruvate and 4-imidazolecarboxaldehyde shows that MppR catalyzes the aldol condensation of these compounds and subsequent dehydration. Surprisingly, the structure of MppR in the presence of "4-hydroxy-2-ketoarginine" shows the correct 4R enantiomer of "2-ketoenduracididine" bound to the enzyme. These data, together with bioinformatic analysis of MppR homologues, identify a novel family within the acetoacetate decarboxylase-like superfamily with divergent active site structure and, consequently, biochemical function.Keywords: Nosocomial infections, Mannopeptimycins, Active site, Gram positive bacteria, Viomycin biosynthesis, X-ray, Protein structure, Reporter group, Glycopeptide antibiotics, Ionization constan
Reducing the environmental impact of surgery on a global scale: systematic review and co-prioritization with healthcare workers in 132 countries
Abstract
Background
Healthcare cannot achieve net-zero carbon without addressing operating theatres. The aim of this study was to prioritize feasible interventions to reduce the environmental impact of operating theatres.
Methods
This study adopted a four-phase Delphi consensus co-prioritization methodology. In phase 1, a systematic review of published interventions and global consultation of perioperative healthcare professionals were used to longlist interventions. In phase 2, iterative thematic analysis consolidated comparable interventions into a shortlist. In phase 3, the shortlist was co-prioritized based on patient and clinician views on acceptability, feasibility, and safety. In phase 4, ranked lists of interventions were presented by their relevance to high-income countries and low–middle-income countries.
Results
In phase 1, 43 interventions were identified, which had low uptake in practice according to 3042 professionals globally. In phase 2, a shortlist of 15 intervention domains was generated. In phase 3, interventions were deemed acceptable for more than 90 per cent of patients except for reducing general anaesthesia (84 per cent) and re-sterilization of ‘single-use’ consumables (86 per cent). In phase 4, the top three shortlisted interventions for high-income countries were: introducing recycling; reducing use of anaesthetic gases; and appropriate clinical waste processing. In phase 4, the top three shortlisted interventions for low–middle-income countries were: introducing reusable surgical devices; reducing use of consumables; and reducing the use of general anaesthesia.
Conclusion
This is a step toward environmentally sustainable operating environments with actionable interventions applicable to both high– and low–middle–income countries
Structural and Functional Characterization of MppR, an Enduracididine Biosynthetic Enzyme from <i>Streptomyces hygroscopicus</i>: Functional Diversity in the Acetoacetate Decarboxylase-like Superfamily
The nonproteinogenic amino acid enduracididine
is a critical component
of the mannopeptimycins, cyclic glycopeptide antibiotics with activity
against drug-resistant pathogens, including methicillin-resistant <i>Staphylococcus aureus</i>. Enduracididine is produced in <i>Streptomyces hygroscopicus</i> by three enzymes, MppP, MppQ,
and MppR. On the basis of primary sequence analysis, MppP and MppQ
are pyridoxal 5′-phosphate-dependent aminotransferases; MppR
shares a low, but significant, level of sequence identity with acetoacetate
decarboxylase. The exact reactions catalyzed by each enzyme and the
intermediates involved in the route to enduracididine are currently
unknown. Herein, we present biochemical and structural characterization
of MppR that demonstrates a catalytic activity for this enzyme and
provides clues about its role in enduracididine biosynthesis. Bioinformatic
analysis shows that MppR belongs to a previously uncharacterized family
within the acetoacetate decarboxylase-like superfamily (ADCSF) and
suggests that MppR-like enzymes may catalyze reactions diverging from
the well-characterized, prototypical ADCSF decarboxylase activity.
MppR shares a high degree of structural similarity with acetoacetate
decarboxylase, though the respective quaternary structures differ
markedly and structural differences in the active site explain the
observed loss of decarboxylase activity. The crystal structure of
MppR in the presence of a mixture of pyruvate and 4-imidazolecarboxaldehyde
shows that MppR catalyzes the aldol condensation of these compounds
and subsequent dehydration. Surprisingly, the structure of MppR in
the presence of “4-hydroxy-2-ketoarginine” shows the
correct 4<i>R</i> enantiomer of “2-ketoenduracididine”
bound to the enzyme. These data, together with bioinformatic analysis
of MppR homologues, identify a novel family within the acetoacetate
decarboxylase-like superfamily with divergent active site structure
and, consequently, biochemical function
Structural and Functional Characterization of MppR, an Enduracididine Biosynthetic Enzyme from <i>Streptomyces hygroscopicus</i>: Functional Diversity in the Acetoacetate Decarboxylase-like Superfamily
The nonproteinogenic amino acid enduracididine
is a critical component
of the mannopeptimycins, cyclic glycopeptide antibiotics with activity
against drug-resistant pathogens, including methicillin-resistant <i>Staphylococcus aureus</i>. Enduracididine is produced in <i>Streptomyces hygroscopicus</i> by three enzymes, MppP, MppQ,
and MppR. On the basis of primary sequence analysis, MppP and MppQ
are pyridoxal 5′-phosphate-dependent aminotransferases; MppR
shares a low, but significant, level of sequence identity with acetoacetate
decarboxylase. The exact reactions catalyzed by each enzyme and the
intermediates involved in the route to enduracididine are currently
unknown. Herein, we present biochemical and structural characterization
of MppR that demonstrates a catalytic activity for this enzyme and
provides clues about its role in enduracididine biosynthesis. Bioinformatic
analysis shows that MppR belongs to a previously uncharacterized family
within the acetoacetate decarboxylase-like superfamily (ADCSF) and
suggests that MppR-like enzymes may catalyze reactions diverging from
the well-characterized, prototypical ADCSF decarboxylase activity.
MppR shares a high degree of structural similarity with acetoacetate
decarboxylase, though the respective quaternary structures differ
markedly and structural differences in the active site explain the
observed loss of decarboxylase activity. The crystal structure of
MppR in the presence of a mixture of pyruvate and 4-imidazolecarboxaldehyde
shows that MppR catalyzes the aldol condensation of these compounds
and subsequent dehydration. Surprisingly, the structure of MppR in
the presence of “4-hydroxy-2-ketoarginine” shows the
correct 4<i>R</i> enantiomer of “2-ketoenduracididine”
bound to the enzyme. These data, together with bioinformatic analysis
of MppR homologues, identify a novel family within the acetoacetate
decarboxylase-like superfamily with divergent active site structure
and, consequently, biochemical function
Structural and Functional Characterization of MppR, an Enduracididine Biosynthetic Enzyme from <i>Streptomyces hygroscopicus</i>: Functional Diversity in the Acetoacetate Decarboxylase-like Superfamily
The nonproteinogenic amino acid enduracididine
is a critical component
of the mannopeptimycins, cyclic glycopeptide antibiotics with activity
against drug-resistant pathogens, including methicillin-resistant <i>Staphylococcus aureus</i>. Enduracididine is produced in <i>Streptomyces hygroscopicus</i> by three enzymes, MppP, MppQ,
and MppR. On the basis of primary sequence analysis, MppP and MppQ
are pyridoxal 5′-phosphate-dependent aminotransferases; MppR
shares a low, but significant, level of sequence identity with acetoacetate
decarboxylase. The exact reactions catalyzed by each enzyme and the
intermediates involved in the route to enduracididine are currently
unknown. Herein, we present biochemical and structural characterization
of MppR that demonstrates a catalytic activity for this enzyme and
provides clues about its role in enduracididine biosynthesis. Bioinformatic
analysis shows that MppR belongs to a previously uncharacterized family
within the acetoacetate decarboxylase-like superfamily (ADCSF) and
suggests that MppR-like enzymes may catalyze reactions diverging from
the well-characterized, prototypical ADCSF decarboxylase activity.
MppR shares a high degree of structural similarity with acetoacetate
decarboxylase, though the respective quaternary structures differ
markedly and structural differences in the active site explain the
observed loss of decarboxylase activity. The crystal structure of
MppR in the presence of a mixture of pyruvate and 4-imidazolecarboxaldehyde
shows that MppR catalyzes the aldol condensation of these compounds
and subsequent dehydration. Surprisingly, the structure of MppR in
the presence of “4-hydroxy-2-ketoarginine” shows the
correct 4<i>R</i> enantiomer of “2-ketoenduracididine”
bound to the enzyme. These data, together with bioinformatic analysis
of MppR homologues, identify a novel family within the acetoacetate
decarboxylase-like superfamily with divergent active site structure
and, consequently, biochemical function
Structural and Functional Characterization of MppR, an Enduracididine Biosynthetic Enzyme from <i>Streptomyces hygroscopicus</i>: Functional Diversity in the Acetoacetate Decarboxylase-like Superfamily
The nonproteinogenic amino acid enduracididine
is a critical component
of the mannopeptimycins, cyclic glycopeptide antibiotics with activity
against drug-resistant pathogens, including methicillin-resistant <i>Staphylococcus aureus</i>. Enduracididine is produced in <i>Streptomyces hygroscopicus</i> by three enzymes, MppP, MppQ,
and MppR. On the basis of primary sequence analysis, MppP and MppQ
are pyridoxal 5′-phosphate-dependent aminotransferases; MppR
shares a low, but significant, level of sequence identity with acetoacetate
decarboxylase. The exact reactions catalyzed by each enzyme and the
intermediates involved in the route to enduracididine are currently
unknown. Herein, we present biochemical and structural characterization
of MppR that demonstrates a catalytic activity for this enzyme and
provides clues about its role in enduracididine biosynthesis. Bioinformatic
analysis shows that MppR belongs to a previously uncharacterized family
within the acetoacetate decarboxylase-like superfamily (ADCSF) and
suggests that MppR-like enzymes may catalyze reactions diverging from
the well-characterized, prototypical ADCSF decarboxylase activity.
MppR shares a high degree of structural similarity with acetoacetate
decarboxylase, though the respective quaternary structures differ
markedly and structural differences in the active site explain the
observed loss of decarboxylase activity. The crystal structure of
MppR in the presence of a mixture of pyruvate and 4-imidazolecarboxaldehyde
shows that MppR catalyzes the aldol condensation of these compounds
and subsequent dehydration. Surprisingly, the structure of MppR in
the presence of “4-hydroxy-2-ketoarginine” shows the
correct 4<i>R</i> enantiomer of “2-ketoenduracididine”
bound to the enzyme. These data, together with bioinformatic analysis
of MppR homologues, identify a novel family within the acetoacetate
decarboxylase-like superfamily with divergent active site structure
and, consequently, biochemical function
Structural and Functional Characterization of MppR, an Enduracididine Biosynthetic Enzyme from <i>Streptomyces hygroscopicus</i>: Functional Diversity in the Acetoacetate Decarboxylase-like Superfamily
The nonproteinogenic amino acid enduracididine
is a critical component
of the mannopeptimycins, cyclic glycopeptide antibiotics with activity
against drug-resistant pathogens, including methicillin-resistant <i>Staphylococcus aureus</i>. Enduracididine is produced in <i>Streptomyces hygroscopicus</i> by three enzymes, MppP, MppQ,
and MppR. On the basis of primary sequence analysis, MppP and MppQ
are pyridoxal 5′-phosphate-dependent aminotransferases; MppR
shares a low, but significant, level of sequence identity with acetoacetate
decarboxylase. The exact reactions catalyzed by each enzyme and the
intermediates involved in the route to enduracididine are currently
unknown. Herein, we present biochemical and structural characterization
of MppR that demonstrates a catalytic activity for this enzyme and
provides clues about its role in enduracididine biosynthesis. Bioinformatic
analysis shows that MppR belongs to a previously uncharacterized family
within the acetoacetate decarboxylase-like superfamily (ADCSF) and
suggests that MppR-like enzymes may catalyze reactions diverging from
the well-characterized, prototypical ADCSF decarboxylase activity.
MppR shares a high degree of structural similarity with acetoacetate
decarboxylase, though the respective quaternary structures differ
markedly and structural differences in the active site explain the
observed loss of decarboxylase activity. The crystal structure of
MppR in the presence of a mixture of pyruvate and 4-imidazolecarboxaldehyde
shows that MppR catalyzes the aldol condensation of these compounds
and subsequent dehydration. Surprisingly, the structure of MppR in
the presence of “4-hydroxy-2-ketoarginine” shows the
correct 4<i>R</i> enantiomer of “2-ketoenduracididine”
bound to the enzyme. These data, together with bioinformatic analysis
of MppR homologues, identify a novel family within the acetoacetate
decarboxylase-like superfamily with divergent active site structure
and, consequently, biochemical function
Structural and Functional Characterization of MppR, an Enduracididine Biosynthetic Enzyme from <i>Streptomyces hygroscopicus</i>: Functional Diversity in the Acetoacetate Decarboxylase-like Superfamily
The nonproteinogenic amino acid enduracididine
is a critical component
of the mannopeptimycins, cyclic glycopeptide antibiotics with activity
against drug-resistant pathogens, including methicillin-resistant <i>Staphylococcus aureus</i>. Enduracididine is produced in <i>Streptomyces hygroscopicus</i> by three enzymes, MppP, MppQ,
and MppR. On the basis of primary sequence analysis, MppP and MppQ
are pyridoxal 5′-phosphate-dependent aminotransferases; MppR
shares a low, but significant, level of sequence identity with acetoacetate
decarboxylase. The exact reactions catalyzed by each enzyme and the
intermediates involved in the route to enduracididine are currently
unknown. Herein, we present biochemical and structural characterization
of MppR that demonstrates a catalytic activity for this enzyme and
provides clues about its role in enduracididine biosynthesis. Bioinformatic
analysis shows that MppR belongs to a previously uncharacterized family
within the acetoacetate decarboxylase-like superfamily (ADCSF) and
suggests that MppR-like enzymes may catalyze reactions diverging from
the well-characterized, prototypical ADCSF decarboxylase activity.
MppR shares a high degree of structural similarity with acetoacetate
decarboxylase, though the respective quaternary structures differ
markedly and structural differences in the active site explain the
observed loss of decarboxylase activity. The crystal structure of
MppR in the presence of a mixture of pyruvate and 4-imidazolecarboxaldehyde
shows that MppR catalyzes the aldol condensation of these compounds
and subsequent dehydration. Surprisingly, the structure of MppR in
the presence of “4-hydroxy-2-ketoarginine” shows the
correct 4<i>R</i> enantiomer of “2-ketoenduracididine”
bound to the enzyme. These data, together with bioinformatic analysis
of MppR homologues, identify a novel family within the acetoacetate
decarboxylase-like superfamily with divergent active site structure
and, consequently, biochemical function