Literature summary for 1.14.14.5 extracted from

Armacost, K.; Musila, J.; Gathiaka, S.; Ellis, H.R.; Acevedo, O.
Exploring the catalytic mechanism of alkanesulfonate monooxygenase using molecular dynamics (2014), Biochemistry, 53, 3308-3317 .

Search for more literature for 1.14.14.5

Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulations for Ssud in substrate-free form, bound with FMNH2, bound with a C4a-peroxyflavin intermediate (FMNOO?), bound with octanesulfonate, cobound with FMNH2 and octanesulfonate, and cobound with FMNOO? and octanesulfonate	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
D111A	kcat/Km vlaue similar to wild-type	Escherichia coli
E20A	kcat/Km vlaue similar to wild-type	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0312	-	octanesulfonate	wild-type, pH 7.5, temperature not specified in the publication	Escherichia coli
0.0322	-	octanesulfonate	mutant E20A, pH 7.5, temperature not specified in the publication	Escherichia coli
0.0363	-	octanesulfonate	mutant D111A, pH 7.5, temperature not specified in the publication	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P80645	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
octanesulfonate + FMNH2 + O2	-	Escherichia coli	octanal + FMN + sulfite + H2O	-	?

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.065	-	octanesulfonate	mutant E20A, pH 7.5, temperature not specified in the publication	Escherichia coli
0.675	-	octanesulfonate	mutant D111A, pH 7.5, temperature not specified in the publication	Escherichia coli
0.73	-	octanesulfonate	wild-type, pH 7.5, temperature not specified in the publication	Escherichia coli

General Information

General Information	Comment	Organism
physiological function	salt bridges between Arg297 and Glu20 or Asp111 are not critical to the desulfonation mechanism. The predicted role of residue Arg297 is to favorably interact with the phosphate group of the reduced flavin. Arg226 functions as a protection group shielding FMNOO- from bulk solvent and is more pronounced when both FMNOO- and octanesulfonate are bound	Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism	Structure
18	-	octanesulfonate	mutant D111A, pH 7.5, temperature not specified in the publication	Escherichia coli
18	-	octanesulfonate	mutant E20A, pH 7.5, temperature not specified in the publication	Escherichia coli
23	-	octanesulfonate	wild-type, pH 7.5, temperature not specified in the publication	Escherichia coli

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Release 2023.1 (January 2023)