Protein Family Models

Squalene-hopene cyclase, EC:5.4.99.17, catalyses the cyclisation of squalene into hopene in bacteria. This reaction is part of a cationic cyclisation cascade, which is homologous to a key step in cholesterol biosynthesis. This family is the C-terminal half of the molecule. [1]. 9931258. The structure of the membrane protein squalene-hopene cyclase at. 2.0 A resolution.. Wendt KU, Lenhart A, Schulz GE;. J Mol Biol. 1999;286:175-187.. [2]. 12747780. Binding structures and potencies of oxidosqualene cyclase. inhibitors with the homologous squalene-hopene cyclase.. Lenhart A, Reinert DJ, Aebi JD, Dehmlow H, Morand OH, Schulz GE;. J Med Chem. 2003;46:2083-2092.. [3]. 12617471. Subcellular localization of oxidosqualene cyclases from. Arabidopsis thaliana, Trypanosoma cruzi, and Pneumocystis. carinii expressed in yeast.. Milla P, Viola F, Oliaro Bosso S, Rocco F, Cattel L, Joubert BM,. LeClair RJ, Matsuda SP, Balliano G;. Lipids. 2002;37:1171-1176. (from Pfam)

Date:

2024-08-14

The activation of homoserine through succinylation of homoserine in some bacteria, such as Escherichia coli and Bacillus cereus, is carried out by homoserine O-succinyltransferase (HTS, EC:2.3.1.46), while other bacteria, such as Haemophilus influenzae, Pseudomonas aeruginosa, and Mycobacterium tuberculosis, acetylate homoserine via homoserine O-acetyltransferase (HTA;EC:2.3.1.31) [1,2]. This family also includes serine acetyltransferase CysE (EC:2.3.1.30) from Lactobacillus casei, which catalyses the formation of O-acetyl serine from L-serine and acetyl-CoA, and is involved in cysteine biosynthesis [3]. [1]. 17442255. Assessing the roles of essential functional groups in the. mechanism of homoserine succinyltransferase.. Coe DM, Viola RE;. Arch Biochem Biophys. 2007;461:211-218.. [2]. 17546672. Crystal structure of homoserine O-succinyltransferase from. Bacillus cereus at 2.4 A resolution.. Zubieta C, Krishna SS, McMullan D, Miller MD, Abdubek P,. Agarwalla S, Ambing E, Astakhova T, Axelrod HL, Carlton D, Chiu. HJ, Clayton T, Deller M, DiDonato M, Duan L, Elsliger MA,. Grzechnik SK, Hale J, Hampton E, Han GW, Haugen J, Jaroszewski. L, Jin KK, Klock HE, Knuth MW, Koesema E, Kumar A, Marciano D,. Morse AT, Nigoghossian E, Oommachen S, Reyes R, Rife CL, van den. Bedem H, Weekes D, White A, Xu Q, Hodgson KO, Wooley J, Deacon. AM, Godzik A, Lesley SA, Wilson IA;. Proteins. 2007;68:999-1005.. [3]. 26790714. Cysteine biosynthesis in Lactobacillus casei: identification and. characterization of a serine acetyltransferase.. Bogicevic B, Berthoud H, Portmann R, Bavan T, Meile L, Irmler S;. FEMS Microbiol Lett. 2016; [Epub ahead of p. TRUNCATED at 1650 bytes (from Pfam)

Date:

2024-08-14

This Pfam entry contains the following members: N-acetyl-glutamine semialdehyde dehydrogenase (AgrC) Aspartate-semialdehyde dehydrogenase [1]. 10369777. Structure of aspartate-beta-semialdehyde dehydrogenase from. Escherichia coli, a key enzyme in the aspartate family of amino. acid biosynthesis.. Hadfield A, Kryger G, Ouyang J, Petsko GA, Ringe D, Viola R;. J Mol Biol 1999;289:991-1002. (from Pfam)

Date:

2024-08-14