Results 151 to 160 of about 537 (173)
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A novel, cupin-type phosphoglucose isomerase in Escherichia coli

Biochimica et Biophysica Acta (BBA) - General Subjects, 2020
Escherichia coli cells contain a homolog of presumed 5-keto-4-deoxyuronate isomerase (KduI) from pectin-degrading soil bacteria, but the catalytic activity of the E. coli protein (o-KduI) was never demonstrated.The known three-dimensional structure of E. coli o-KduI was compared with the available structures of sugar-converting enzymes.
Natalia N, Vorobjeva   +6 more
openaire   +2 more sources

[Evolution of seed storage globulins and cupin superfamily].

Molekuliarnaia biologiia, 2011
An extensive superfamily of cupins (clan cl09118) currently combines thousands of functionally and structurally diverse prokaryote and eukaryote proteins, which contain a beta-barrel of antiparallel beta-strands (cupin module). Possible ways of the formation of the cupin superfamily were suggested based on the comparison of primary and tertiary ...
A D, Shutov, I A, Kakhovskaia
openaire   +3 more sources

A cupin domain is involved in α-amylase inhibitory activity

Plant Science, 2018
Proteinaceous α-amylase inhibitors have specialized activities that make some strong inhibition of α-amylases. New α-amylase inhibitors continue to be discovered so far. A proteinaceous α-amylase inhibitor CL-AI was isolated and identified from chickpea seeds.
Zhankui, Wang   +14 more
openaire   +2 more sources

Catalytic diversity of cupin domain-containing enzymes

2018
<p>Cupins are a large superfamily of enzymatic and non-enzymatic members that contain a conserved β-barrel domain, or double-stranded β-helix (DSBH) fold. The cupin superfamily is one of the most functionally diverse groups of proteins known to exist.
Nicholas Jay Schnicker   +5 more
openaire   +1 more source

A Well-Defined Osmium–Cupin Complex: Hyperstable Artificial Osmium Peroxygenase

Journal of the American Chemical Society, 2017
Thermally stable TM1459 cupin superfamily protein from Thermotoga maritima was repurposed as an osmium (Os) peroxygenase by metal-substitution strategy employing the metal-binding promiscuity. This novel artificial metalloenzyme bears a datively bound Os ion supported by the 4-histidine motif.
Nobutaka Fujieda   +8 more
openaire   +2 more sources

A Cupin Epoxidase Catalyzes Epoxycyclohexenone Formation in Fungal Meroterpenoid Biosynthesis

Organic Letters
We identified the par biosynthetic gene cluster from Paraphaeosphaeria sp. C-XB-J-1, responsible for producing epoxycyclohexenone (ECH)-containing meroterpenoids, paraphaeones. In vitro reconstitution revealed the sequential action of the cupin-domain protein ParE and the SDR enzyme ParD in ECH formation.
Yun-Tao Jiang   +7 more
openaire   +2 more sources

Dynamic properties of the layers of cupin-1.1 aggregates at the air/water interface

Biophysical Chemistry
Spread layers of amorphous aggregates of the structural domain of plant protein vicilin, cupin-1.1, at the water - air interface were studied by the surface tensiometry, dilational surface rheology, Brewster angle and atomic force microscopy. The layer properties differed strongly from the results for the layers of previously studied proteins.
Nikolay A, Isakov   +3 more
openaire   +2 more sources

Cupin-1.1 Adsorption Layers at the Surface of 8 M Urea Solutions

The Journal of Physical Chemistry B
The adsorption layers of cupin-1.1, one of the two evolutionary conserved β-barrel domains of vicilin─the garden pea storage globulin─at the liquid-gas interface were studied by a few methods of the surface chemistry. The kinetic dependencies of the surface pressure of cupin-1.1 solutions in 8 M urea overlap in a single master curve if the surface ...
Nikolay A. Isakov   +6 more
openaire   +2 more sources

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