Gcvh

H Multiple mitochondrial dysfunctions syndrome. MLEU:

High-resolution three-dimensional structures of essential Mycobacterium tuberculosis Mtb proteins provide templates for TB drug design, but are available for only a small fraction of the Mtb proteome. Here we evaluate an intra-genus "homolog-rescue" strategy to increase the structural information available for TB drug discovery by using mycobacterial homologs with conserved active sites. Of potential TB drug targets selected for x-ray structure determination, only 16 yielded a crystal structure. By adding homologs from nine other mycobacterial species to the pipeline, structures representing an additional 52 otherwise intractable targets were solved. To determine whether these homolog structures would be useful surrogates in TB drug design, we compared the active sites of pairs of Mtb and non-TB mycobacterial NTM enzyme homologs with experimentally determined structures, using three metrics of active site similarity, including superposition of continuous pharmacophoric property distributions. The utility of these structures in TB drug design can be tested by designing inhibitors using the homolog structure and assaying the cognate Mtb enzyme; a promising test case, Mtb cytidylate kinase, is described. The homolog-rescue strategy evaluated here for TB is also generalizable to drug targets for other diseases.

Gcvh

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CTUL: gcshb.

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Lipoic acid is synthesized by a remarkably atypical pathway in which the cofactor is assembled on its cognate proteins. An octanoyl moiety diverted from fatty acid synthesis is covalently attached to the acceptor protein, and sulfur insertion at carbons 6 and 8 of the octanoyl moiety form the lipoyl cofactor. Covalent attachment of this cofactor is required for function of several central metabolism enzymes, including the glycine cleavage H protein GcvH. In Bacillus subtilis , GcvH is the sole substrate for lipoate assembly. Hence lipoic acid-requiring 2-oxoacid dehydrogenase OADH proteins acquire the cofactor only by transfer from lipoylated GcvH. Lipoyl transfer has been argued to be the primordial pathway of OADH lipoylation. Because roughly 3 billion years separate the divergence of these bacteria, it is surprising that E. Known and putative GcvHs from other bacteria and eukaryotes also substitute for B. Because glycine cleavage is the primary GcvH role in ancestral bacteria that lack OADH enzymes, lipoyl transfer is a "moonlighting" function: that is, development of a new function while retaining the original function. This moonlighting has been conserved in the absence of selection by some, but not all, GcvH proteins.

Gcvh

PCC substr. Jiyao W et al. Conserved Protein Domain Family gcvH. TIGR gcvH Download alignment glycine cleavage system H protein This model represents the glycine cleavage system H protein, which shuttles the methylamine group of glycine from the P protein to the T protein.

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CCAN: Gcsh. OFU: IEL: LSQ: VRA: MESC: SLUC: gcshb CANN: TNL: DMN: DGT: H Multiple mitochondrial dysfunctions syndrome. ESP:

Glycine cleavage complex H protein GcvH is one of the four components that form the glycine cleavage complex GCS , essential for the synthesis of C 1 one-carbon units for cell metabolism, by the oxidative cleavage of glycine. The activity of this complex is induced in the presence of exogenous glycine, and is repressed by purines.

GAB: AFZ: HRJ: PVIR: LWE: lwe gcvH. DVI: EPA: VUM: OGL: SVS: PBAR: CIN: