Literature summary for 4.1.2.19 extracted from

Kroemer, M.; Merkel, I.; Schulz, G.E.
Structure and catalytic mechanism of L-rhamnulose-1-phosphate aldolase (2003), Biochemistry, 42, 10560-10568.

Crystallization (Commentary)

Crystallization (Comment)	Organism
structure established at 1.35 A resolution in a crystal form that is obtained by a surface mutation and has one subunit of the C4-symmetric tetramer in the asymmetric unit. Crystals of the wild-type enzyme with their 20 crystallographically asymmetric subunits diffract to only 2.7 A resolution are much too complex for a convenient analysis of structural modifications. For both reasons, a more suitable crystal form is obtained by producing the six point mutants W8T, Q51R, Q52E, D98Y, E192A and E254R at the protein surface far away from the active center	Escherichia coli

Crystallization (Comment)

Organism

structure established at 1.35 A resolution in a crystal form that is obtained by a surface mutation and has one subunit of the C4-symmetric tetramer in the asymmetric unit. Crystals of the wild-type enzyme with their 20 crystallographically asymmetric subunits diffract to only 2.7 A resolution are much too complex for a convenient analysis of structural modifications. For both reasons, a more suitable crystal form is obtained by producing the six point mutants W8T, Q51R, Q52E, D98Y, E192A and E254R at the protein surface far away from the active center

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
E117Q	0.1% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 0.04% of the wild-type ratio	Escherichia coli
E171A	0.4% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 0.3% of the wild-type ratio	Escherichia coli
E171Q	0.4% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 0.1% of the wild-type ratio	Escherichia coli
E171S	2% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 0.7% of the wild-type ratio	Escherichia coli
E192A	as active as the wild-type enzyme with L-rhamnulose 1-phosphate	Escherichia coli
G264Stop	75% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as 23% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 7% of the wild-type ratio	Escherichia coli
N29A	4% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 0.9% of the wild-type ratio	Escherichia coli
R28S	9% of the activity of the wild-type enzyme with L-rhamnulose 1-phosphate as substrate, the ratio of turnover number to Km-value is 2% of the wild-type ratio	Escherichia coli

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P32169	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Escherichia coli

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
L-Rhamnulose 1-phosphate	-	Escherichia coli	Glycerone phosphate + (S)-lactaldehyde	-	?