Literature summary for 1.5.1.3 extracted from

Penhallurick, R.; Durnal, M.; Harold, A.; Ichiye, T.
Adaptations for pressure and temperature in dihydrofolate reductases (2021), Microorganisms, 9, 1706 .

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Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	-	-	-
Moritella yayanosii	-	-	-

General Information

General Information	Comment	Organism
evolution	replacement of Asp27 in Escherichia coli DHFR by Glu27 in Moritella DHFR may be an adaptation for cold that fortuitously also enhances activity under pressure. The extra carbon of a glutamate increases flexibility of the Thr113-Res27 hydrogen bond while pressure increases the hydrogen bond strength and correlation of sheet F with helix B	Escherichia coli
evolution	Tyr103 of Moritella yayanosii DHFR may be an adaptation for high pressure since Cys103 in helix F of Moritella profunda DHFR forms an intra-helix hydrogen bond with Ile99 while Tyr103 in helix F of MyDHFR forms a hydrogen bond with Leu78 in helix E. Tyr 103 may be an adaptation for preventing distortion of the adenosine binding domain at higher pressures that may only be advantageous for cold-adapted DHFRs	Moritella yayanosii

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Release 2023.1 (January 2023)