EC number:4.2.1.168

Enzyme

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     4. Lyases
        4.2 Carbon-oxygen lyases
            4.2.1 Hydro-lyases
ID:4.2.1.168
Description:GDP-4-dehydro-6-deoxy-alpha-D-mannose 3-dehydratase.
Cath: 3.40.640.10; 3.90.1150.10;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 4.2.1.168
BRENDA Enzyme Link: BRENDA 4.2.1.168
KEGG Enzyme Link: KEGG4.2.1.168
BioCyc Enzyme Link: BioCyc 4.2.1.168
ExPASy Enzyme Link: ExPASy4.2.1.168
EC2PDB Enzyme Link: EC2PDB 4.2.1.168
ExplorEnz Enzyme Link: ExplorEnz 4.2.1.168
PRIAM enzyme-specific profiles Link: PRIAM 4.2.1.168
IntEnz Enzyme Link: IntEnz 4.2.1.168
MEDLINE Enzyme Link: MEDLINE 4.2.1.168

EC number:4.2.1.168

MSA:

4.2.1.168;
Phylogenetic Tree:

4.2.1.168;
Uniprot:
M-CSA:
RHEA:49488 GDP-4-dehydro-alpha-D-rhamnose + L-glutamate = 2-oxoglutarate + GDP-4-dehydro-3,6-dideoxy-alpha-D-mannose + NH4(+)
RULE(radius=1) [*:1]-[CH;+0:2](-[*:3])-[NH2;+0:4].[*:5]-[CH;+0:6](-[*:7])-[OH;+0:8]>>[*:1]-[C;H0;+0:2](-[*:3])=[O;H0;+0:8].[*:5]-[CH2;+0:6]-[*:7].[NH3;+0:4]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Biosynthesis of colitose: expression, purification, and mechanistic characterization of GDP-4-keto-6-deoxy-D-mannose-3-dehydrase (ColD) and GDP-L-colitose synthase (ColC).Alam J, Beyer N, Liu HW2004 Dec 2815610039
A structural study of GDP-4-keto-6-deoxy-D-mannose-3-dehydratase: caught in the act of geminal diamine formation.Cook PD, Holden HM2007 Dec 1117997582