Protein Family Models

This domain corresponds to an amidase function. Many of these proteins are involved in cell wall metabolism of bacteria. This domain is found at the N-terminus of Swiss:P43675, where it functions as a glutathionylspermidine amidase EC:3.5.1.78 [1]. This domain is found to be the catalytic domain of PlyCA [4]. CHAP is the amidase domain of bifunctional Escherichia coli glutathionylspermidine synthetase/amidase, and it catalyses the hydrolysis of Gsp (glutathionylspermidine) into glutathione and spermidine [5]. [1]. 7775463. Glutathionylspermidine metabolism in Escherichia coli.. Purification, cloning, overproduction, and characterization of a. bifunctional glutathionylspermidine synthetase/amidase.. Bollinger JM Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT;. J Biol Chem 1995;270:14031-14041.. [2]. 12765834. The CHAP domain: a large family of amidases including GSP. amidase and peptidoglycan hydrolases.. Bateman A, Rawlings ND;. Trends Biochem Sci 2003;28:234-237.. [3]. 12765833. Amidase domains from bacterial and phage autolysins define a. family of gamma-D,L-glutamate-specific amidohydrolases.. Rigden DJ, Jedrzejas MJ, Galperin MY;. Trends Biochem Sci 2003;28:230-234.. [4]. 16818874. PlyC: a multimeric bacteriophage lysin.. Nelson D, Schuch R, Chahales P, Zhu S, Fischetti VA;. Proc Natl Acad Sci U S A. 2006;103:10765-10770.. [5]. 21226054. Structure and mechanism of Escherichia coli. glutathionylspermidine amidase belonging to the family of. cysteine; histidine-dependent amidohydrolases/peptidases.. Pai CH, Wu HJ, Lin CH, Wang AH;. Protein Sci. 2011;20:557-566. (from Pfam)

Date:

2024-08-14

This region contains the Glutathionylspermidine synthase enzymatic activity EC:6.3.1.8. This is the C-terminal region in bi-enzymes such as Swiss:P43675. Glutathionylspermidine (GSP) synthetases of Trypanosomatidae and Escherichia coli couple hydrolysis of ATP (to ADP and Pi) with formation of an amide bond between spermidine and the glycine carboxylate of glutathione (gamma-Glu-Cys-Gly). In the pathogenic trypanosomatids, this reaction is the penultimate step in the biosynthesis of the antioxidant metabolite, trypanothione (N1,N8-bis-(glutathionyl)spermidine), and is a target for drug design [1]. This region, the pre-ATP grasp region, probably carries the substrate-binding site [2]. [1]. 7775463. Glutathionylspermidine metabolism in Escherichia coli.. Purification, cloning, overproduction, and characterization of a. bifunctional glutathionylspermidine synthetase/amidase.. Bollinger JM Jr, Kwon DS, Huisman GW, Kolter R, Walsh CT;. J Biol Chem 1995;270:14031-14041.. [2]. 17124497. Dual binding sites for translocation catalysis by Escherichia. coli glutathionylspermidine synthetase.. Pai CH, Chiang BY, Ko TP, Chou CC, Chong CM, Yen FJ, Chen S,. Coward JK, Wang AH, Lin CH;. EMBO J. 2006;25:5970-5982. (from Pfam)

Date:

2024-08-14

bifunctional glutathionylspermidine amidase/synthetase catalyzes the formation of glutathionylspermidine from glutathione and spermidine; also catalyzes the reverse reaction

Date:

2018-07-25

Gene:

gss

Date:

2020-10-26