1lkc
From Proteopedia
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==Function== | ==Function== | ||
| - | [[http://www.uniprot.org/uniprot/COBD_SALTY COBD_SALTY]] Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.<ref>PMID:9446573</ref> | + | [[http://www.uniprot.org/uniprot/COBD_SALTY COBD_SALTY]] Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.<ref>PMID:9446573</ref> |
==About this Structure== | ==About this Structure== | ||
Revision as of 01:35, 4 April 2013
Contents |
Crystal Structure of L-Threonine-O-3-Phosphate Decarboxylase from Salmonella enterica
Template:ABSTRACT PUBMED 11939774
Function
[COBD_SALTY] Decarboxylates L-threonine-O-3-phosphate to yield (R)-1-amino-2-propanol O-2-phosphate, the precursor for the linkage between the nucleotide loop and the corrin ring in cobalamin.[1]
About this Structure
1lkc is a 1 chain structure with sequence from Salmonella enterica. This structure supersedes the now removed PDB entry 1kus. Full crystallographic information is available from OCA.
Reference
- Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I. Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica. Biochemistry. 2002 Apr 16;41(15):4798-808. PMID:11939774
- ↑ Brushaber KR, O'Toole GA, Escalante-Semerena JC. CobD, a novel enzyme with L-threonine-O-3-phosphate decarboxylase activity, is responsible for the synthesis of (R)-1-amino-2-propanol O-2-phosphate, a proposed new intermediate in cobalamin biosynthesis in Salmonella typhimurium LT2. J Biol Chem. 1998 Jan 30;273(5):2684-91. PMID:9446573
