Sustainability of supply or the planet: a review of potential drop-in alternative aviation fuels

Rye, Lucas; Blakey, Simon; Wilson, C. W.

doi:10.1039/b918197k

Cited by 129 publications

(87 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…1A) (22,23). In the x-ray crystal structure of A-CAT, residues 806 -841 lack defined electron density and thus form a disordered C-terminal tail (C-tail) (23).…”

Section: Resultsmentioning

confidence: 99%

“…DNA constructs encoding site-directed mutants of A-CAT were generated using the QuikChange XL site-directed mutagenesis system (Stratagene). Constructs were cloned in-frame into the NcoI and XhoI sites of the pET-28a vector (Novagen) to add an N-terminal His tag and a TEV protease site as described (23). Fulllength MHCK A constructs (NCBI accession XP_635600) were cloned into the plasmid pTX-FLAG vector (28) that had been adapted to GATEWAY technology (Invitrogen).…”

Section: Methodsmentioning

confidence: 99%

“…To model the C-tail at the P i -pocket, the protocol was constrained to force the phosphate group of Thr 825 to create similar hydrogen bonds and salt bridges as the original P i molecule solved in the crystal structure. To model the C-tail at the active site a soft constraint was imposed in the initial low resolution step that required that the C␤ atom of Thr 825 be within 3-6 Å of the C␤ atom of Asp 756 , which is presumed to act as the catalytic base in the phosphotransferase reaction (23). This constraint was removed in the subsequent highresolution modeling steps of all three stages.…”

Section: Crystallization Procedures and Data Collection And Analysis-mentioning

confidence: 99%

“…The xray crystal structure of A-CAT reveals that it is composed of an N-terminal and C-terminal lobe with the active site situated in a cleft at the interface between the two lobes (23). An invariant catalytic residue in the active site (Asp 766 ) can be phosphorylated, suggesting that the ␣-kinase catalytic mecha-nism differs from that of conventional eukaryotic protein kinases.…”

mentioning

confidence: 99%

“…The Mg 2ϩ binding sites are regulatory, because millimolar concentrations of Mg 2ϩ , in excess of that required to bind to ATP, are required for A-CAT to exhibit maximal catalytic activity (22). A-CAT also binds a P i molecule at a highly basic site in the C-terminal lobe that we term the P i -pocket (23).…”

mentioning

confidence: 99%

See 4 more Smart Citations

Autophosphorylation Activates Dictyostelium Myosin II Heavy Chain Kinase A by Providing a Ligand for an Allosteric Binding Site in the α-Kinase Domain

Crawley

Gharaei

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

Dictyostelium discoideum myosin II heavy chain kinase A (MHCK A), a member of the atypical ␣-kinase family, phosphorylates sites in the myosin II tail that block filament assembly. Here we show that the catalytic activity of A-CAT, the ␣-kinase domain of MHCK A (residues 552-841), is severely inhibited by the removal of a disordered C-terminal tail sequence (C-tail; residues 806 -841). The key residue in the C-tail was identified as Thr 825 , which was found to be constitutively autophosphorylated. Dephosphorylation of Thr 825 using shrimp alkaline phosphatase decreased A-CAT activity. The activity of a truncated A-CAT lacking Thr 825 could be rescued by P i , phosphothreonine, and a phosphorylated peptide, but not by threonine, glutamic acid, aspartic acid, or an unphosphorylated peptide. These results focused attention on a P i -binding pocket located in the C-terminal lobe of A-CAT. Mutational analysis demonstrated that the P ipocket was essential for A-CAT activity. Based on these results, it is proposed that autophosphorylation of Thr 825 activates ACAT by providing a covalently tethered ligand for the P i -pocket. Ab initio modeling studies using the Rosetta FloppyTail and FlexPepDock protocols showed that it is feasible for the phosphorylated Thr 825 to dock intramolecularly into the P i -pocket. Allosteric activation is predicted to involve a conformational change in Arg 734, which bridges the bound P i to Asp 762 in a key active site loop. Sequence alignments indicate that a comparable regulatory mechanism is likely to be conserved in Dictyostelium MHCK B-D and metazoan eukaryotic elongation factor-2 kinases.Dictyostelium discoideum MHCK A 3 is a highly specialized protein kinase that targets three threonine residues located in the ␣-helical coiled-coil tail of myosin II (1-4). Phosphorylation of these sites results in the disassembly of myosin II bipolar filaments and inhibits processes, such as cytokinesis, that depend on myosin II contractile activity (5, 6). MHCK A is 130-kDa in size and consists of an N-terminal ␣-helical coiled-coil domain, a central kinase domain, and a C-terminal WD-repeat domain (7). The coiled-coil domain assembles into trimers or tetramers, binds, and cross-links actin filaments and is responsible for targeting MHCK A to actin-rich cellular protrusions (8 -10). The WD-repeat domain interacts with filamentous myosin II and is required for MHCK A to efficiently phosphorylate myosin II (10, 11). The kinase domain of MHCK A bears no sequence similarity to the superfamily of "conventional" eukaryotic protein kinases but instead belongs to a small but widespread family of atypical protein kinases termed the ␣-kinases (12).In addition to MHCK A, D. discoideum expresses five proteins with ␣-kinase domains. Three of the proteins, termed MHCK B, C, and D, are closely related to MHCK A and at least two to them, MHCK B and C, function cooperatively to regulate myosin II filament assembly in vivo (13-15). The other two ␣-kinases, AK1 and VwkA, have domain structures unrelated to MHCK A...

show abstract

“…1A) (22,23). In the x-ray crystal structure of A-CAT, residues 806 -841 lack defined electron density and thus form a disordered C-terminal tail (C-tail) (23).…”

Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Crystallization Procedures and Data Collection And Analysis-mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Autophosphorylation Activates Dictyostelium Myosin II Heavy Chain Kinase A by Providing a Ligand for an Allosteric Binding Site in the α-Kinase Domain

Crawley

Gharaei

et al. 2011

Journal of Biological Chemistry

View full text Add to dashboard Cite

show abstract

Power‐to‐Liquids ‐ Conversion ofCO₂and Renewable H₂to Methanol

White¹

2022

Advances in Energy Storage

View full text Add to dashboard Cite

Hydroconversion of Waste Cooking Oil into Bio‐Jet Fuel over a Hierarchical NiMo/USY@Al‐SBA‐15 Zeolite

et al. 2018

View full text Add to dashboard Cite

The direct conversion of waste cooking oil (WCO) into bio-jet fuel was investigated over a core-shell hierarchical USY@Al-SBA-15 zeolite-supported NiMo catalyst. The core-shell structure showed better acid and pore size distributions. The synergetic effect of the core-shell micropore and mesopore structure significantly contributed to enhancing the selectivity for the jet fuel (C 9-15 hydrocarbons) from 9.3 % over NiMo/USY up to 35.7 % over NiMo/USY@Al-SBA-15, with high isomerization (iso-/n-paraffins ratio = 2.7) and moderate aromatic fraction (18.7 %). The decarboxylation reaction was selectively enhanced. Optimal selectivity for jet fuel (39.7 %) was obtained at 380°C and a high H 2 /oil ratio would decrease the yield of jet fuel. This catalyst showed excellent stability for the hydroconversion of WCO to hydrocarbons.

show abstract

Sustainability of supply or the planet: a review of potential drop-in alternative aviation fuels

Cited by 129 publications

References 19 publications

Autophosphorylation Activates Dictyostelium Myosin II Heavy Chain Kinase A by Providing a Ligand for an Allosteric Binding Site in the α-Kinase Domain

Autophosphorylation Activates Dictyostelium Myosin II Heavy Chain Kinase A by Providing a Ligand for an Allosteric Binding Site in the α-Kinase Domain

Power‐to‐Liquids ‐ Conversion ofCO₂and Renewable H₂to Methanol

Hydroconversion of Waste Cooking Oil into Bio‐Jet Fuel over a Hierarchical NiMo/USY@Al‐SBA‐15 Zeolite

Contact Info

Product

Resources

About

Sustainability of supply or the planet: a review of potential drop-in alternative aviation fuels

Cited by 129 publications

References 19 publications

Autophosphorylation Activates Dictyostelium Myosin II Heavy Chain Kinase A by Providing a Ligand for an Allosteric Binding Site in the α-Kinase Domain

Autophosphorylation Activates Dictyostelium Myosin II Heavy Chain Kinase A by Providing a Ligand for an Allosteric Binding Site in the α-Kinase Domain

Power‐to‐Liquids ‐ Conversion ofCO2and Renewable H2to Methanol

Hydroconversion of Waste Cooking Oil into Bio‐Jet Fuel over a Hierarchical NiMo/USY@Al‐SBA‐15 Zeolite

Contact Info

Product

Resources

About

Power‐to‐Liquids ‐ Conversion ofCO₂and Renewable H₂to Methanol