Literature summary for 1.14.14.5 extracted from

Thakur, A.; Somai, S.; Yue, K.; Ippolito, N.; Pagan, D.; Xiong, J.; Ellis, H.R.; Acevedo, O.
Substrate-dependent mobile loop conformational changes in alkanesulfonate monooxygenase from accelerated molecular dynamics (2020), Biochemistry, 59, 3582-3593 .

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Crystallization (Commentary)

Crystallization (Comment)	Organism
molecular dynamics simulations of wild-type SsuD and variant enzymes bound with different combinations of FMNH2, C4a-peroxyflavin intermediate FMNOO-, and octanesulfonate. Mobile loop conformations are open, closed, and semiclosed. The substrate-free SsuD system has a wide opening capable of providing full access for substrates to enter the active site. Upon binding FMNH2, SsuD adopts a closed conformation. Salt bridges, Asp111-Arg263 and Glu205-Arg271, are particularly important in maintaining the closed conformation. With both FMNH2 and octanesulfonate bound in SsuD, a second conformation is formed dependent upon a favorable pi-pi interaction between residues His124 and Phe261	Escherichia coli

Crystallization (Comment)

Organism

molecular dynamics simulations of wild-type SsuD and variant enzymes bound with different combinations of FMNH2, C4a-peroxyflavin intermediate FMNOO-, and octanesulfonate. Mobile loop conformations are open, closed, and semiclosed. The substrate-free SsuD system has a wide opening capable of providing full access for substrates to enter the active site. Upon binding FMNH2, SsuD adopts a closed conformation. Salt bridges, Asp111-Arg263 and Glu205-Arg271, are particularly important in maintaining the closed conformation. With both FMNH2 and octanesulfonate bound in SsuD, a second conformation is formed dependent upon a favorable pi-pi interaction between residues His124 and Phe261

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
F261W	complete loss of activity	Escherichia coli
R263A	similar kinetic parameters as wild-type	Escherichia coli
R263A/R271A	similar kinetic parameters as wild-type	Escherichia coli
R271A	mutation does not alter the catalytic activity, but in the presence of reduced flavin the variant is more susceptible to proteolytic digestion compared to wild-type	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism
0.05	-	octanesulfonate	wild-type, pH 7.5, 25°C	Escherichia coli
0.057	-	octanesulfonate	mutant R271A, pH 7.5, 25°C	Escherichia coli
0.113	-	octanesulfonate	mutant R263A/R271A, pH 7.5, 25°C	Escherichia coli
0.235	-	octanesulfonate	mutant R263A, pH 7.5, 25°C	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	-	?

Synonyms

Synonyms	Comment	Organism
SsuD	-	Escherichia coli
YcbN	-	Escherichia coli

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism
0.84	-	octanesulfonate	wild-type, pH 7.5, 25°C	Escherichia coli
1.03	-	octanesulfonate	mutant R263A, pH 7.5, 25°C	Escherichia coli
1.1	-	octanesulfonate	mutant R263A/R271A, pH 7.5, 25°C	Escherichia coli
1.4	-	octanesulfonate	mutant R271A, pH 7.5, 25°C	Escherichia coli

kcat/KM [mM/s]

kcat/KM Value [1/mMs^-1]	kcat/KM Value Maximum [1/mMs^-1]	Substrate	Comment	Organism
4.4	-	octanesulfonate	mutant R263A, pH 7.5, 25°C	Escherichia coli
10	-	octanesulfonate	mutant R263A/R271A, pH 7.5, 25°C	Escherichia coli
17	-	octanesulfonate	wild-type, pH 7.5, 25°C	Escherichia coli
25	-	octanesulfonate	mutant R271A, pH 7.5, 25°C	Escherichia coli