|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
Enzymes and Genes:
|Pseudomonas denitrificans:||threonine-phosphate decarboxylase: cobC|
|Salmonella enterica enterica serovar Typhimurium:||L-threonine-O-3-phosphate decarboxylase: cobD|
In Pathway: aminopropanol phosphate biosynthesis I
The direction shown, i.e. which substrates are on the left and right sides, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: threonine-phosphate decarboxylase
Enzyme Commission Synonyms: L-threonine-O-3-phosphate decarboxylase, CobD, L-threonine-O-3-phosphate carboxy-lyase
Standard Gibbs Free Energy (ΔrG'°): -1.8418121 kcal/mol [Latendresse13]
Enzyme Commission Summary:
This enzyme is unable to decarboxylate the D-isomer of threonine
Brushaber98: Brushaber KR, O'Toole GA, Escalante-Semerena JC (1998). "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 273(5);2684-91. PMID: 9446573
Cheong02: Cheong CG, Bauer CB, Brushaber KR, Escalante-Semerena JC, Rayment I (2002). "Three-dimensional structure of the L-threonine-O-3-phosphate decarboxylase (CobD) enzyme from Salmonella enterica." Biochemistry 41(15);4798-808. PMID: 11939774
©2016 SRI International, 333 Ravenswood Avenue, Menlo Park, CA 94025-3493