Literature summary for 4.1.2.13 extracted from

Pezza, J.A.; Stopa, J.D.; Brunyak, E.M.; Allen, K.N.; Tolan, D.R.
Thermodynamic analysis shows conformational coupling and dynamics confer substrate specificity in fructose-1,6-bisphosphate aldolase (2007), Biochemistry, 46, 13010-13018.

Search for more literature for 4.1.2.13

Cloned(Commentary)

Cloned (Comment)	Organism
expressed in Escherichia coli	Oryctolagus cuniculus

Inhibitors

Inhibitors	Comment	Organism	Structure
CuSO4	0.02 mM, inactivation	Oryctolagus cuniculus
o-phenanthroline	0.06 mM, inactivation	Oryctolagus cuniculus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.0095	-	D-fructose 1,6-bisphosphate	at 30°C	Oryctolagus cuniculus
40	-	D-Fructose 1-phosphate	at 30°C	Oryctolagus cuniculus

Organism

Organism	UniProt	Comment	Textmining
Oryctolagus cuniculus	P00883	-	-

Purification (Commentary)

Purification (Comment)	Organism
CM-Sepharose CL-6B chromatography	Oryctolagus cuniculus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
D-fructose 1,6-bisphosphate	-	Oryctolagus cuniculus	glycerone phosphate + D-glyceraldehyde 3-phosphate	-	?
D-Fructose 1-phosphate	-	Oryctolagus cuniculus	Glycerone phosphate + D-glyceraldehyde	-	?

Synonyms

Synonyms	Comment	Organism
aldolase A	-	Oryctolagus cuniculus

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
0.63	-	D-Fructose 1-phosphate	at 30°C	Oryctolagus cuniculus
10.2	-	D-fructose 1,6-bisphosphate	at 30°C	Oryctolagus cuniculus

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)