KEGG   ENZYME: 4.3.1.30Help
Entry
EC 4.3.1.30                 Enzyme                                 

Name
dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase;
desII (gene name);
eryCV (gene name);
MegCV
Class
Lyases;
Carbon-nitrogen lyases;
Ammonia-lyases
BRITE hierarchy
Sysname
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose ammonia lyase (dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose-forming)
Reaction(IUBMB)
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose + S-adenosyl-L-methionine + reduced acceptor = dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose + NH3 + L-methionine + 5'-deoxyadenosine + acceptor [RN:R08583]
Reaction(KEGG)
Substrate
dTDP-4-amino-4,6-dideoxy-alpha-D-glucopyranose [CPD:C04268];
S-adenosyl-L-methionine [CPD:C00019];
reduced acceptor [CPD:C00030]
Product
dTDP-3-dehydro-4,6-dideoxy-alpha-D-glucopyranose [CPD:C11909];
NH3 [CPD:C00014];
L-methionine [CPD:C00073];
5'-deoxyadenosine [CPD:C05198];
acceptor [CPD:C00028]
Comment
The enzyme, which is a member of the 'AdoMet radical' (radical SAM) family, is involved in biosynthesis of TDP-alpha-D-desosamine. The reaction starts by the transfer of an electron from the reduced form of the enzyme's [4Fe-4S] cluster to S-adenosyl-L-methionine, spliting it into methionine and the radical 5-deoxyadenosin-5'-yl, which attacks the sugar substrate.
History
EC 4.3.1.30 created 2011
Pathway
ec00523  Polyketide sugar unit biosynthesis
ec01100  Metabolic pathways
ec01130  Biosynthesis of antibiotics
Orthology
K13309  dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase
Genes
STRE: GZL_03702
STRM: M444_29865
SNR: SNOUR_10125(eryCV)
AER: AERYTH_15835
SEN: SACE_0715(eryCV)
AEY: CDG81_13215(desII)
Taxonomy
Reference
1  [PMID:19746907]
  Authors
Szu PH, Ruszczycky MW, Choi SH, Yan F, Liu HW
  Title
Characterization and mechanistic studies of DesII: a radical S-adenosyl-L-methionine enzyme involved in the biosynthesis of TDP-D-desosamine.
  Journal
J Am Chem Soc 131:14030-42 (2009)
DOI:10.1021/ja903354k
Reference
2  [PMID:20121093]
  Authors
Ruszczycky MW, Choi SH, Liu HW
  Title
Stoichiometry of the redox neutral deamination and oxidative dehydrogenation reactions catalyzed by the radical SAM enzyme DesII.
  Journal
J Am Chem Soc 132:2359-69 (2010)
DOI:10.1021/ja909451a
Reference
3  [PMID:21513273]
  Authors
Ruszczycky MW, Choi SH, Mansoorabadi SO, Liu HW
  Title
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.
  Journal
J Am Chem Soc 133:7292-5 (2011)
DOI:10.1021/ja201212f
Other DBs
ExplorEnz - The Enzyme Database: 4.3.1.30
IUBMB Enzyme Nomenclature: 4.3.1.30
ExPASy - ENZYME nomenclature database: 4.3.1.30
BRENDA, the Enzyme Database: 4.3.1.30

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