4 research outputs found
Data_Sheet_1_Inter-hospital transfer in patients with acute myocardial infarction in China: Findings from the improving care for cardiovascular disease in China-acute coronary syndrome project.PDF
BackgroundLittle is known about the current scenario of inter-hospital transfer for patients with acute myocardial infarction (AMI) in China.MethodsFrom November 2014 to December 2019, 94,623 AMI patients were enrolled from 241 hospitals in 30 provinces in China. We analyzed the pattern of inter-hospital transfer, and compared in-hospital treatments and outcomes between transferred patients and directly admitted patients.ResultsOf these patients, 40,970 (43.3%) were transferred from hospitals that did not provide percutaneous coronary intervention (PCI). The proportion of patients who were transferred from non-PCI hospital was 46.3% and 11.9% (P ConclusionMore than 40% of the hospitalized AMI patients were transferred from non-PCI-capable hospitals in China. Further strategies are needed to enhance the capability of revascularization and reduce the inequality in management of AMI.</p
Glycyl Radical Enzymes Catalyzing the Dehydration of Two Isomers of <i>N</i>‑Methyl-4-hydroxyproline
The
various isomers of hydroxyproline (HP) are widely
distributed
in nature, serving as key components of structural proteins, while
their quaternized betaine derivatives function as osmoprotectants
in many organisms. Aerobic bacteria degrade HPs through a variety
of well-studied mechanisms. Recent studies show that certain anaerobic
bacteria degrade HPs through distinct mechanisms, involving the O2-sensitive glycyl radical enzymes (GREs) t4L-HP dehydratase
(HypD) and t4D-HP C–N lyase (HplG). Here, we report the discovery
of two more GREs, N-methyl c4L-HP dehydratase (HpyG)
and N-methyl c4D-HP dehydratase (HpzG), which catalyze
radical-mediated dehydration of the two N-methyl-c4HP
enantiomers, while also displaying significant activities toward their
unmethylated substrates. Both GREs are associated with homologues
of pyrroline-5-carboxylate reductase, which catalyze reduction of
their products N-methyl-pyrroline-5-carboxylate to
form N-methyl-proline. Crystal structures of HpyG
and HpzG in complex with their substrates revealed active site architectures
distinct from that of HypD and provided insights into the mechanism
of enantioselective radical-mediated dehydration. Our research further
expands the repertoire of diverse chemical mechanisms involved in
the bacterial metabolism of highly prevalent HP isomers and derivatives
in the anaerobic biosphere
Glycyl Radical Enzymes Catalyzing the Dehydration of Two Isomers of <i>N</i>‑Methyl-4-hydroxyproline
The
various isomers of hydroxyproline (HP) are widely
distributed
in nature, serving as key components of structural proteins, while
their quaternized betaine derivatives function as osmoprotectants
in many organisms. Aerobic bacteria degrade HPs through a variety
of well-studied mechanisms. Recent studies show that certain anaerobic
bacteria degrade HPs through distinct mechanisms, involving the O2-sensitive glycyl radical enzymes (GREs) t4L-HP dehydratase
(HypD) and t4D-HP C–N lyase (HplG). Here, we report the discovery
of two more GREs, N-methyl c4L-HP dehydratase (HpyG)
and N-methyl c4D-HP dehydratase (HpzG), which catalyze
radical-mediated dehydration of the two N-methyl-c4HP
enantiomers, while also displaying significant activities toward their
unmethylated substrates. Both GREs are associated with homologues
of pyrroline-5-carboxylate reductase, which catalyze reduction of
their products N-methyl-pyrroline-5-carboxylate to
form N-methyl-proline. Crystal structures of HpyG
and HpzG in complex with their substrates revealed active site architectures
distinct from that of HypD and provided insights into the mechanism
of enantioselective radical-mediated dehydration. Our research further
expands the repertoire of diverse chemical mechanisms involved in
the bacterial metabolism of highly prevalent HP isomers and derivatives
in the anaerobic biosphere
Glycyl Radical Enzymes Catalyzing the Dehydration of Two Isomers of <i>N</i>‑Methyl-4-hydroxyproline
The
various isomers of hydroxyproline (HP) are widely
distributed
in nature, serving as key components of structural proteins, while
their quaternized betaine derivatives function as osmoprotectants
in many organisms. Aerobic bacteria degrade HPs through a variety
of well-studied mechanisms. Recent studies show that certain anaerobic
bacteria degrade HPs through distinct mechanisms, involving the O2-sensitive glycyl radical enzymes (GREs) t4L-HP dehydratase
(HypD) and t4D-HP C–N lyase (HplG). Here, we report the discovery
of two more GREs, N-methyl c4L-HP dehydratase (HpyG)
and N-methyl c4D-HP dehydratase (HpzG), which catalyze
radical-mediated dehydration of the two N-methyl-c4HP
enantiomers, while also displaying significant activities toward their
unmethylated substrates. Both GREs are associated with homologues
of pyrroline-5-carboxylate reductase, which catalyze reduction of
their products N-methyl-pyrroline-5-carboxylate to
form N-methyl-proline. Crystal structures of HpyG
and HpzG in complex with their substrates revealed active site architectures
distinct from that of HypD and provided insights into the mechanism
of enantioselective radical-mediated dehydration. Our research further
expands the repertoire of diverse chemical mechanisms involved in
the bacterial metabolism of highly prevalent HP isomers and derivatives
in the anaerobic biosphere