EC Number   |
General Information |
Reference  |
|---|
    2.8.1.11 | malfunction |
in the moeBA228T mutant strain F36, anaerobic respiratory growth is possible on nitrate but not on DMSO, the cofactor insertion mutation affects the respiratory membrane-bound molybdoenzyme nitrate reductase A (NarGHI), but not respiratory membrane-bound molybdoenzyme dimethylsulfoxide reductase (DmsABC) |
721512 |
| 2.8.1.11 | more |
maturation of the holoenzyme is not cofactor-insertion dependent |
721512 |
| 2.8.1.11 | physiological function |
MoeB functions to sulfurylate MoaD, and in the structure of the MoeB-MoaD complex, Ala228 is located in the interface region between the two proteins |
721512 |
| 2.8.1.11 | more |
the recombinant His6-tagged MOCS3-RLD is partially gluconoylated at the N-terminus which results in a heterogeneity of the protein but does not influence sulfurtransferase activity |
721600 |
| 2.8.1.11 | physiological function |
the human MOCS3 protein contains a C-terminal segment displaying similarities to the sulfurtransferase rhodanese. MOCS3 catalyzes both the adenylation and the subsequent generation of a thiocarboxylate group at the C-terminus of the smaller subunit of molybdopterin, MPT, synthase during molybdenum cofactor biosynthesis in humans. The N-terminus of MOCS3 is expected to activate the C-terminal glycine of, MOCS2A to form an acyl adenylate. Subsequently, the C-terminal rhodanese-like domain (RLD) of MOCS3 acts as a direct sulfur donor for the formation of a thiocarboxylate group on MOCS2A, The MOCS2A thiocarboxylate sulfur is used for the generation of the dithiolene moiety of molybdopterin which coordinates the molybdenum atom in molybdenum cofactor. The enzyme is able to provide the sulfur for the thiocarboxylation of MOCS2A in a defined in vitro system for the generation of MPT from precursor Z |
721600 |
| 2.8.1.11 | evolution |
MOCS3 belongs to the class of rhodaneses that is found in combination with another protein domain, and contains one rhodanese domain of 158 amino acids at the C-terminus with a sequence identity of less than 20% with the classic two-domain rhodaneses, phylogenetic analysis of MoeB homologues, overview |
722226 |
| 2.8.1.11 | metabolism |
the enzyme is involved in the biosynthesis of the molybdenum cofactor divided into three steps: conversion of GTP to precursor, transformation of the precursor to molybdopterin, and insertion of molybdenum into MPT to form the molybdenum cofactor |
722226 |
| 2.8.1.11 | more |
the MOCS3 C-terminal domain is homologous to rhodanese-like proteins. The last amino acid must be either polar or positively charged to increase the thiosulfate sulfurtransferase activity of MOCS3-RLD |
722226 |
| 2.8.1.11 | physiological function |
molybdopterin synthase sulfurase is involved in sulfur transfer to the C-terminus of the molybdopterin synthase, which synthesizes the molybdenum cofactor, that play a central role in several enzymes, role of specific conserved residues in the six amino acid active site loop of MOCS3-RLD in thiosulfate sulfurtransferase activity |
722226 |
| 2.8.1.11 | more |
the enzyme contains two potential nucleotide binding Gly-rich motifs (Gly-X-Gly-X-X-Gly) starting at residue positions 173 and 189 |
722607 |
