Results 21 to 30 of about 3,408 (192)

Heterologous gene expression and characterization of two serine hydroxymethyltransferases from Thermoplasma acidophilum

open access: yes, 2021
Ma’ruf IF, Sasaki Y, Kerbs A, et al. Heterologous gene expression and characterization of two serine hydroxymethyltransferases from Thermoplasma acidophilum. Extremophiles.
Ma’ruf, Ilma Fauziah   +24 more
core   +1 more source

Thermoplasma acidophilum TAA43 is an archaeal member of the eukaryotic meiotic branch of AAA ATPases [PDF]

open access: yes, 2004
Sequencing of the Thermoplasma acidophilum genome revealed a new gene, taa43 , which codes for a 43-kDa protein containing one AAA domain; we therefore termed it Thermoplasma AAA ATPase of 43 kDa (TAA43). Close homologs of TAA43 are found only in related
Jürgen Peters   +17 more
core   +2 more sources

Refolding of a thermostable glyceraldehyde dehydrogenase for application in synthetic cascade biomanufacturing. [PDF]

open access: yesPLoS ONE, 2013
The production of chemicals from renewable resources is gaining importance in the light of limited fossil resources. One promising alternative to widespread fermentation based methods used here is Synthetic Cascade Biomanufacturing, the application of ...
Fabian Steffler, Volker Sieber
doaj   +1 more source

Human Naa50 Shows Serotonin N-Acetyltransferase Activity, and Its Overexpression Enhances Melatonin Biosynthesis, Resulting in Osmotic Stress Tolerance in Rice

open access: yesAntioxidants, 2023
A new clade of serotonin N-acetyltransferase (SNAT), the penultimate enzyme in the melatonin biosynthetic pathway, has been reported in the archaeon Thermoplasma volcanium.
Kyungjin Lee, Kyoungwhan Back
doaj   +1 more source

Escherichia coli RimI Encodes Serotonin N-Acetyltransferase Activity and Its Overexpression Leads to Enhanced Growth and Melatonin Biosynthesis

open access: yesBiomolecules, 2023
Serotonin N-acetyltransferase (SNAT) functions as the penultimate or final enzyme in melatonin biosynthesis, depending on the substrate. The Escherichia coli orthologue of archaeal SNAT from Thermoplasma volcanium was identified as RimI (EcRimI), with 42%
Kyungjin Lee, Kyoungwhan Back
doaj   +1 more source

Cryo-EM single particle analysis with the Volta phase plate

open access: yeseLife, 2016
We present a method for in-focus data acquisition with a phase plate that enables near-atomic resolution single particle reconstructions. Accurate focusing is the determining factor for obtaining high quality data.
Radostin Danev, Wolfgang Baumeister
doaj   +1 more source

Structure of a AAA+ unfoldase in the process of unfolding substrate

open access: yeseLife, 2017
AAA+ unfoldases are thought to unfold substrate through the central pore of their hexameric structures, but how this process occurs is not known.
Zev A Ripstein   +4 more
doaj   +1 more source

The Intein of the Thermoplasma A-ATPase A Subunit: Structure, Evolution and Expression in E. Coli [PDF]

open access: yes, 2001
Inteins are selfish genetic elements that excise themselves from the host protein during post translational processing, and religate the host protein with a peptide bond.
Alireza G Senejani   +5 more
core   +1 more source

2.8 Å resolution reconstruction of the Thermoplasma acidophilum 20S proteasome using cryo-electron microscopy

open access: yeseLife, 2015
Recent developments in detector hardware and image-processing software have revolutionized single particle cryo-electron microscopy (cryoEM) and led to a wave of near-atomic resolution (typically ∼3.3 Å) reconstructions.
Melody G Campbell   +4 more
doaj   +1 more source

Ultrastructure of lipopolysaccharide isolated from Thermoplasma acidophilum [PDF]

open access: yesJournal of Bacteriology, 1975
The fine structure of lipopolysaccharide isolated from Thermoplasma acidophilum was examined by electron microscopy. Negative staining of the lipopolysaccharide revealed long, ribbon-like structures with some branching. The average width of the lipopolysaccharide ribbons was 5 nm.
K J, Mayberry-Carson   +2 more
openaire   +2 more sources

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