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Homocitrate synthase post-HMGL domain-like
alpha-isopropylmalate synthase regulatory domain-containing protein
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)
HMGL-like
This family contains a diverse set of enzymes. These include various aldolases and a region of pyruvate carboxylase. (from Pfam)
2-isopropylmalate synthase
2-isopropylmalate synthase converts acetyl-CoA and alpha-ketoisovalerate into alpha-isopropylmalate in the committed step of leucine biosynthesis
This is the first enzyme of leucine biosynthesis. 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 found primarily in Bacteria. The homologous families in the Archaea may represent isozymes and/or related enzymes.
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