Literature summary for 1.1.1.28 extracted from

Furukawa, N.; Miyanaga, A.; Nakajima, M.; Taguchi, H.
Structural basis of sequential allosteric transitions in tetrameric D-lactate dehydrogenases from three Gram-negative bacteria (2018), Biochemistry, 57, 5388-5406 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
comparison of the apo and ternary complex structures of Fusobacterium nucleatum FnLDH and Escherichia coli EcLDH and Pseudomonas aeruginosa PaLDH. FnLDH and EcLDH exhibit positive cooperativity in substrate binding, and PaLDH shows negatively cooperative substrate binding. The three enzymes consistently form homotetrameric structures with three symmetric axes, the P-, Q-, and R-axes, which allows apo-FnLDH and EcLDH to form wide intersubunit contact surfaces between the opened catalytic domains of the two Q-axis-related subunits in coordination with their asymmetric and distorted quaternary structures. apo-PaLDH possesses a highly symmetrical quaternary structure and partially closed catalytic domains that are favorable for initial substrate binding and forms virtually no intersubunit contact surface between the catalytic domains	Fusobacterium nucleatum subsp. nucleatum
comparison of the apo and ternary complex structures of Fusobacterium nucleatum FnLDH and Escherichia coli EcLDH and Pseudomonas aeruginosa PaLDH. FnLDH and EcLDH exhibit positive cooperativity in substrate binding, and PaLDH shows negatively cooperative substrate binding. The three enzymes consistently form homotetrameric structures with three symmetric axes, the P-, Q-, and R-axes, which allows apo-FnLDH and EcLDH to form wide intersubunit contact surfaces between the opened catalytic domains of the two Q-axis-related subunits in coordination with their asymmetric and distorted quaternary structures. apo-PaLDH possesses a highly symmetrical quaternary structure and partially closed catalytic domains that are favorable for initial substrate binding and forms virtually no intersubunit contact surface between the catalytic domains	Pseudomonas aeruginosa
comparison of the apo and ternary complex structures of Fusobacterium nucleatum FnLDH and Escherichia coli EcLDH and Pseudomonas aeruginosa PaLDH. FnLDH and EcLDH exhibit positive cooperativity in substrate binding, and PaLDH shows negatively cooperative substrate binding. The three enzymes consistently form homotetrameric structures with three symmetric axes, the P-, Q-, and R-axes, which allows apo-FnLDH and EcLDH to form wide intersubunit contact surfaces between the opened catalytic domains of the two Q-axis-related subunits in coordination with their asymmetric and distorted quaternary structures. apo-PaLDH possesses a highly symmetrical quaternary structure and partially closed catalytic domains that are favorable for initial substrate binding and forms virtually no intersubunit contact surface between the catalytic domains	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	A0A140N893	-	-
Escherichia coli BL21-DE3	A0A140N893	-	-
Fusobacterium nucleatum subsp. nucleatum	Q8RG11	-	-
Fusobacterium nucleatum subsp. nucleatum DSM 15643	Q8RG11	-	-
Pseudomonas aeruginosa	Q9I530	-	-
Pseudomonas aeruginosa DSM 22644	Q9I530	-	-

Synonyms

Synonyms	Comment	Organism
ECBD_2243	-	Escherichia coli
FN0511	-	Fusobacterium nucleatum subsp. nucleatum
LdhA	-	Pseudomonas aeruginosa

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Release 2023.1 (January 2023)