EC number:1.1.99.38

Enzyme

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     1. Oxidoreductases
        1.1 Acting on the CH-OH group of donors
            1.1.99 With unknown physiological acceptors
ID:1.1.99.38
Description:2-deoxy-scyllo-inosamine dehydrogenase (AdoMet-dependent).
Cath: 3.20.20.70;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 1.1.99.38
BRENDA Enzyme Link: BRENDA 1.1.99.38
KEGG Enzyme Link: KEGG1.1.99.38
BioCyc Enzyme Link: BioCyc 1.1.99.38
ExPASy Enzyme Link: ExPASy1.1.99.38
EC2PDB Enzyme Link: EC2PDB 1.1.99.38
ExplorEnz Enzyme Link: ExplorEnz 1.1.99.38
PRIAM enzyme-specific profiles Link: PRIAM 1.1.99.38
IntEnz Enzyme Link: IntEnz 1.1.99.38
MEDLINE Enzyme Link: MEDLINE 1.1.99.38

EC number:1.1.99.38

MSA:

1.1.99.38;
Phylogenetic Tree:

1.1.99.38;
Uniprot:
M-CSA:
RHEA:34275 2-deoxy-scyllo-inosamine + S-adenosyl-L-methionine = 3-amino-2,3-dideoxy-scyllo-inosose + 5'-deoxyadenosine + H(+) + L-methionine
RULE(radius=1) [*:1]-[CH2;+0:2]-[S+;H0:3](-[*:4])-[*:5].[*:6]-[CH;+0:7](-[*:8])-[OH;+0:9]>>[*:6]-[C;H0;+0:7](-[*:8])=[O;H0;+0:9].[*:1]-[CH3;+0:2].[*:4]-[S;H0;+0:3]-[*:5]
Reaction
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References

TitleAuthorsDatePubMed ID
Mechanistic study on the reaction of a radical SAM dehydrogenase BtrN by electron paramagnetic resonance spectroscopy.Yokoyama K, Ohmori D, Kudo F, Eguchi T2008 Aug 2618672902
Characterization and mechanistic study of a radical SAM dehydrogenase in the biosynthesis of butirosin.Yokoyama K, Numakura M, Kudo F, Ohmori D, Eguchi T2007 Dec 1218001019