Publications

• Crystal structure of 2-phosphosulfolactate phosphatase (ComB) from Clostridium acetobutylicum at 2.6 A resolution reveals a new fold with a novel active site.

  DiDonato M., Krishna S.S., Schwarzenbacher R., McMullan D., Agarwalla S., Brittain S.M., Miller M.D., Abdubek P., Ambing E., Axelrod H.L., Canaves J.M., Chiu H.J., Deacon A.M., Duan L., Elsliger M.A., Godzik A., Grzechnik S.K., Hale J., Hampton E., Haugen J., Jaroszewski L., Jin K.K., Klock H.E., Knuth M.W., Koesema E., Kreusch A., Kuhn P., Lesley S.A., Levin I., Morse A.T., Nigoghossian E., Okach L., Oommachen S., Paulsen J., Quijano K., Reyes R., Rife C.L., Spraggon G., Stevens R.C., van den Bedem H., White A., Wolf G., Xu Q., Hodgson K.O., Wooley J., Wilson I.A.

  Proteins 65:771-776(2006) [PubMed] [EuropePMC]

• Identification of coenzyme M biosynthetic 2-phosphosulfolactate phosphatase. A member of a new class of Mg2+-dependent acid phosphatases.

  Graham D.E., Graupner M., Xu H., White R.H.

  Coenzyme M (CoM; 2-mercaptoethanesulfonic acid) is the terminal methyl carrier in methanogenesis. Methanogenic archaea begin the production of this essential cofactor by sulfonating phosphoenolpyruvate to form 2-phospho-3-sulfolactate. After dephosphorylation, this precursor is oxidized, decarboxy ... >> More

  Coenzyme M (CoM; 2-mercaptoethanesulfonic acid) is the terminal methyl carrier in methanogenesis. Methanogenic archaea begin the production of this essential cofactor by sulfonating phosphoenolpyruvate to form 2-phospho-3-sulfolactate. After dephosphorylation, this precursor is oxidized, decarboxylated and then reductively thiolated to form CoM. A thermostable phosphosulfolactate phosphohydrolase (EC 3.1.3.-) catalyzing the second step in CoM biosynthesis, was identified in the hyperthermophilic euryarchaeon Methanococcus jannaschii. The predicted ORF MJ1140 in the genome of M. jannaschii encodes ComB, a Mg2+-dependent acid phosphatase that is specific for 2-hydroxycarboxylic acid phosphate esters. Recombinantly expressed purified ComB efficiently hydrolyzes rac-2-phosphosulfolactate, (S)-2-phospholactate, phosphoglycolate and both enantiomers of 2-phosphomalate. In contrast to previously studied phosphoglycolate phosphatases, ComB has a low pH optimum for activity, a narrow substrate specificity and an amino acid sequence dissimilar to any biochemically characterized protein. Like other phosphatases that function via covalent phosphoenzyme intermediates, ComB can catalyze a transphosphorylation reaction. Homologs of comB are identified in all available cyanobacterial genome sequences and in genomes from phylogenetically diverse bacteria and archaea; most of these organisms lack homologs of other CoM biosynthetic genes. The broad and disparate distribution of comB homologs suggests that the gene has been recruited frequently into new metabolic pathways. << Less

  Eur. J. Biochem. 268:5176-5188(2001) [PubMed] [EuropePMC]