EC number:4.1.2.13

Enzyme

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     4. Lyases
        4.1 Carbon-carbon lyases
            4.1.2 Aldehyde-lyases
ID:4.1.2.13
Description:Fructose-bisphosphate aldolase.
Alternative Name: Fructose-1,6-bisphosphate triosephosphate-lyase.
D-fructose-1,6-bisphosphate D-glyceraldehyde-3-phosphate-lyase.
Aldolase.
Prosite: PDOC00523; PDOC00143;
PDB:
PDBScop
5GK5 8031183; 8043561; 8031183; 8043561; 8031183; 8043561; 8031183; 8043561; 8031183; 8043561; 8031183; 8043561; 8031183; 8043561; 8031183; 8043561;
5VJE 8031183; 8043561; 8031183; 8043561;
5VJD 8031183; 8043561; 8031183; 8043561;
5GK8 8031183; 8043561; 8031183; 8043561;
5GK7 8031183; 8043561; 8031183; 8043561;
 » show all
Cath: 1.10.150.240; 1.20.5.2750; 3.20.20.70; 3.90.1410.10; 3.90.1420.10; 3.40.50.1000;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.1.2.13
BRENDA Enzyme Link: BRENDA 4.1.2.13
KEGG Enzyme Link: KEGG4.1.2.13
BioCyc Enzyme Link: BioCyc 4.1.2.13
ExPASy Enzyme Link: ExPASy4.1.2.13
EC2PDB Enzyme Link: EC2PDB 4.1.2.13
ExplorEnz Enzyme Link: ExplorEnz 4.1.2.13
PRIAM enzyme-specific profiles Link: PRIAM 4.1.2.13
IntEnz Enzyme Link: IntEnz 4.1.2.13
MEDLINE Enzyme Link: MEDLINE 4.1.2.13

EC number:4.1.2.13

MSA:

4.1.2.13;
Phylogenetic Tree:

4.1.2.13;
Uniprot:
M-CSA:
RHEA:14729 beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate
RULE(radius=1) [*:1]-[C;H0;+0:2]1(-[*:3])-[O;H0;+0:4]-[CH;+0:5](-[*:6])-[CH;+0:7](-[*:8])-[CH;+0:9]-1-[OH;+0:10]>>[*:8]-[CH2;+0:7]-[C;H0;+0:5](-[*:6])=[O;H0;+0:4].[*:1]-[CH;+0:2](-[*:3])-[CH;+0:9]=[O;H0;+0:10]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Active site remodeling during the catalytic cycle in metal-dependent fructose-1,6-bisphosphate aldolases.Jacques B, Coinçon M, Sygusch J2018 May 1829593097
Structural insights into the substrate binding and stereoselectivity of giardia fructose-1,6-bisphosphate aldolase.Galkin A, Li Z, Li L, Kulakova L, Pal LR, Dunaway-Mariano D, Herzberg O2009 Apr 1419236002
Exploring substrate binding and discrimination in fructose1, 6-bisphosphate and tagatose 1,6-bisphosphate aldolases.Zgiby SM, Thomson GJ, Qamar S, Berry A2000 Mar10712619
Cloning, sequence analysis and over-expression of the gene for the class II fructose 1,6-bisphosphate aldolase of Escherichia coli.Alefounder PR, Baldwin SA, Perham RN, Short NJ1989 Jan 152649077