Acetolactate synthase

10994216136ENSG00000105135ENSMUSG00000032763A1L0T0E9PL44Q8BU33NM_006844NM_176826NM_173751NM_001359301NM_001359302NM_001359303NP_006835NP_776112NP_001346230NP_001346231NP_001346232The acetolactate synthase (ALS) enzyme (also known as acetohydroxy acid synthase, or AHAS) is a protein found in plants and micro-organisms. ALS catalyzes the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine). The acetolactate synthase (ALS) enzyme (also known as acetohydroxy acid synthase, or AHAS) is a protein found in plants and micro-organisms. ALS catalyzes the first step in the synthesis of the branched-chain amino acids (valine, leucine, and isoleucine). A human protein of yet unknown function, sharing some sequence similarity with bacterial ALS, is encoded by the ILVBL (ilvB-like) gene. Human ILVBL gene has 17 exons resides on chromosome 19 at q13.1. The catalylic peptide of ALS in mouse-eared cress is a chloroplastic protein consisting of 670 residues, the last 615 of which form the active form. Three main domains are found, with two thiamine pyrophosphate sandwiching a DHS-like NAD/FAD-binding domain. In SCOP assignment, these subunits are named d1yhya1, d1yhya2, and d1yhya3 from the N-terminal to the C-termianl.