Enzyme

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     4. Lyases
        4.3 Carbon-nitrogen lyases
            4.3.1 Ammonia-lyases
ID:4.3.1.30
Description:dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase.

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 4.3.1.30
BRENDA Enzyme Link: BRENDA 4.3.1.30
KEGG Enzyme Link: KEGG4.3.1.30
BioCyc Enzyme Link: BioCyc 4.3.1.30
ExPASy Enzyme Link: ExPASy4.3.1.30
EC2PDB Enzyme Link: EC2PDB 4.3.1.30
ExplorEnz Enzyme Link: ExplorEnz 4.3.1.30
PRIAM enzyme-specific profiles Link: PRIAM 4.3.1.30
IntEnz Enzyme Link: IntEnz 4.3.1.30
MEDLINE Enzyme Link: MEDLINE 4.3.1.30
MSA:

4.3.1.30;

Phylogenetic Tree:

4.3.1.30;

Uniprot:
M-CSA:
RHEA:39647 AH2 + dTDP-4-amino-4,6-dideoxy-alpha-D-glucose + S-adenosyl-L-methionine = 5'-deoxyadenosine + A + dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucose + H(+) + L-methionine + NH4(+)
RULE(radius=1) [*:1]-[CH;+0:2](-[NH2;+0:3])-[CH;+0:4](-[*:5])-[OH;+0:6].[*:7]-[S+;H0:8](-[*:9])-[CH2;+0:10]-[*:11]>>[*:1]-[CH2;+0:2]-[C;H0;+0:4](-[*:5])=[O;H0;+0:6].[*:11]-[CH3;+0:10].[*:7]-[S;H0;+0:8]-[*:9].[NH3;+0:3]
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References

TitleAuthorsDatePubMed ID
Mechanistic studies of the radical S-adenosyl-L-methionine enzyme DesII: EPR characterization of a radical intermediate generated during its catalyzed dehydrogenation of TDP-D-quinovose.Ruszczycky MW, Choi SH, Mansoorabadi SO, Liu HW2011 May 1821513273
Stoichiometry of the redox neutral deamination and oxidative dehydrogenation reactions catalyzed by the radical SAM enzyme DesII.Ruszczycky MW, Choi SH, Liu HW2010 Feb 2420121093
Characterization and mechanistic studies of DesII: a radical S-adenosyl-L-methionine enzyme involved in the biosynthesis of TDP-D-desosamine.Szu PH, Ruszczycky MW, Choi SH, Yan F, Liu HW2009 Oct 719746907