KEGG ENZYME: 4.3.1.30

ENZYME: 4.3.1.30

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

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)

R08583

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

ec01110

Biosynthesis of secondary metabolites

Orthology

K13309

dTDP-4-amino-4,6-dideoxy-D-glucose ammonia-lyase

Genes

SCYE:

R2B67_24625(desII)

STRE:

GZL_03702

STRM:

M444_29865

SNR:	SNOUR_10125(eryCV)

SGF:	HEP81_07916(desII)

SGX:	H4W23_25495(desII)

SATA:

C5746_38525(desII)

SROI:

IAG44_15960(desII)

SHK:	J2N69_01050(desII)

SGK:	PET44_28285(desII)

SYUN:

MOV08_16380(desII)

AER:	AERYTH_15835

SEN:	SACE_0715(eryCV)

MCAB:

HXZ27_06185(rosR)

AEY:	CDG81_13215(desII)

» show all

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

LinkDB

DBGET integrated database retrieval system