Literature summary for 1.3.5.2 extracted from

Couto, S.G.; Cristina Nonato, M.; Costa-Filho, A.J.
Site directed spin labeling studies of Escherichia coli dihydroorotate dehydrogenase N-terminal extension (2011), Biochem. Biophys. Res. Commun., 414, 487-492.

Search for more literature for 1.3.5.2

Protein Variants

Protein Variants	Comment	Organism
F21C/R1C	mutant incorporates into 1-dipalmitoyl-2-oleoyl-sn-glycero-3-phosphocholine/Triton X-100 mixed vesicles and expected to be located right in the core of the more hydrophobic region of the model membrane. Mutated amino acids are either in a strongly immobilized regime or subjected to a fast motion	Escherichia coli
F5C/R1C	mutant incorporates into 1-dipalmitoyl-2-oleoyl-sn-glycero-3-phosphocholine/Triton X-100 mixed vesicles. Mutated residues experience a high degree of freedom that is compatible with their location in the beginning of the protein chain. Mutated amino acids are either in a strongly immobilized regime or subjected to a fast motion	Escherichia coli
H19C/R1C	mutant incorporates into 1-dipalmitoyl-2-oleoyl-sn-glycero-3-phosphocholine/Triton X-100 mixed vesicles and expected to be located right in the core of the more hydrophobic region of the model membrane. Mutated amino acids are either in a strongly immobilized regime or subjected to a fast motion	Escherichia coli
Y2C/R1C	mutant incorporates into 1-dipalmitoyl-2-oleoyl-sn-glycero-3-phosphocholine/Triton X-100 mixed vesicles. Mutated residues experience a high degree of freedom that is compatible with their location in the beginning of the protein chain	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
membrane	electron spin resonance spectra show that the N-terminal binds to membranes and experiences a somewhat high flexibility that could be related to the role of this region as a molecular lid controlling the entrance of the enzyme's active site and thus allowing the enzyme to give access to quinones that are dispersed in the membrane and that are necessary for the catalysis	Escherichia coli	16020	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	B1X8P9	-	-

Synonyms

Synonyms	Comment	Organism
DHODH	-	Escherichia coli

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Release 2023.1 (January 2023)