1lc5

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Template:STRUCTURE 1lc5

Contents 1 Crystal Structure of L-Threonine-O-3-phosphate Decarboxylase from S. enterica in its apo state 2 Function 3 About this Structure 4 Reference

Crystal Structure of L-Threonine-O-3-phosphate Decarboxylase from S. enterica in its apo state

Template:ABSTRACT PUBMED 12119022

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

1lc5 is a 1 chain structure with sequence from Salmonella enterica. Full crystallographic information is available from OCA.

Reference

• Cheong CG, Escalante-Semerena JC, Rayment I. Structural studies of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica: the apo, substrate, and product-aldimine complexes. Biochemistry. 2002 Jul 23;41(29):9079-89. PMID:12119022

1. ↑ 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