Protein Family Models

This entry represents domain found in homologues of alpha-isopropylmalate synthase (IPMS). This domain follows the catalytic domain and is required for the enzymatic activity [3]. Paper describing PDB structure 1sr9. [1]. 15159544. Crystal structure of LeuA from Mycobacterium tuberculosis, a key enzyme in leucine biosynthesis. Koon N, Squire CJ, Baker EN;. Proc Natl Acad Sci U S A 2004;101:8295-8300. Paper describing PDB structure 3hpx. [2]. 22352945. Removal of the C-terminal regulatory domain of alpha-isopropylmalate synthase disrupts functional substrate binding. Huisman FH, Koon N, Bulloch EM, Baker HM, Baker EN, Squire CJ, Parker EJ;. Biochemistry. 2012;51:2289-2297. Paper describing PDB structure 4ov4. [3]. 25128527. Subdomain II of alpha-isopropylmalate synthase is essential for activity: inferring a mechanism of feedback inhibition. Zhang Z, Wu J, Lin W, Wang J, Yan H, Zhao W, Ma J, Ding J, Zhang P, Zhao GP;. J Biol Chem. 2014;289:27966-27978. (from Pfam)

Date:

2024-10-16

This is the C-terminal regulatory (R) domain of alpha-isopropylmalate synthase, which catalyses the first committed step in the leucine biosynthetic pathway [1]. This domain, is an internally duplicated structure with a novel fold [1]. It comprises two similar units that are arranged such that the two -helices pack together in the centre, crossing at an angle of 34 degrees, sandwiched between the two three-stranded, antiparallel beta-sheets. The overall domain is thus constructed as a beta-alpha-beta three-layer sandwich [1]. [1]. 15159544. Crystal structure of LeuA from Mycobacterium tuberculosis, a key enzyme in leucine biosynthesis. Koon N, Squire CJ, Baker EN;. Proc Natl Acad Sci U S A 2004;101:8295-8300. (from Pfam)

Date:

2024-10-16

This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase. (from Pfam)

Date:

2024-11-05

2-isopropylmalate synthase catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate)

Date:

2024-11-06

Date:

2020-10-26

A larger family of homologous proteins includes homocitrate synthase, distinct lineages of 2-isopropylmalate synthase, several distinct, uncharacterized, orthologous sets in the Archaea, and other related enzymes. This model describes a family of 2-isopropylmalate synthases as found in yeasts and in a minority of studied bacteria.

Gene:

leuA

Date:

2021-04-27