EC Number   |
Cofactor |
Reference |
|---|
    4.1.99.22 | Fe-S center |
CNX2/MOCS1A is an FeS enzyme depending on two Fe4S4 clusters, which are assembled by the mitochondrial FeS cluster assembly pathway |
747034 |
| 4.1.99.22 | iron-sulfur centre |
binds 1 4Fe-4S cluster coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine and 1 4Fe-4S cluster coordinated with 3 cysteines and the GTP-derived substrate |
716730 |
| 4.1.99.22 | iron-sulfur centre |
contains two oxygen-sensitive FeS clusters, each coordinated by three cysteine residues. A redox-active [4Fe-4S]2+ cluster is ligated by an N-terminal CX3CX2C motif as is the case with all other D-adenosylmethionione-dependent radical enzymes investigated thus far. A C-terminal CX2CX13C motif that is unique to MOCS1A and its orthologs primarily ligates a [3Fe-4S] cluster. MOCS1A can be reconstituted in vitro under anaerobic conditions to yield a form containing two [4Fe-4S]2+ clusters. The N-terminal [4Fe-4S]2+ cluster is rapidly degraded by oxygen via a semistable [2Fe-2S]2+ cluster intermediate, and the C-terminal [4Fe-4S]2+ cluster is rapidly degraded by oxygen to yield a semistable [3Fe-4S] cluster intermediate |
715468 |
| 4.1.99.22 | iron-sulfur centre |
MoaA harbors an N-terminal [4Fe-4S] cluster, which is involved in the reductive cleavage of S-adenosyl-L-methionine and generates a 5'-deoxyadenosyl radical, and a C-terminal [4Fe-4S] cluster presumably involved in substrate binding andor activation. MoaA binds 5'-GTP with high affinity and interacts through its C-terminal [4Fe-4S] cluster with the guanine N1 and N2 atoms |
716738 |
| 4.1.99.22 | iron-sulfur centre |
the enzyme contains iron-sulfur centres |
714999 |
| 4.1.99.22 | S-adenosyl-L-methionine |
MoaA as a radical S-adenosyl-L-methionine enzyme |
727694 |
| 4.1.99.22 | S-adenosyl-L-methionine |
MoaA is a radical S-adenosylmethionine (SAM) enzyme |
727013 |
| 4.1.99.22 | S-adenosyl-L-methionine |
MoaAis a radical S-adenosyl-L-methionine (SAM) enzyme. S-adenosyl-L-methionine serves as the free radical initiator and undergoes cleavage to methionine and a 5'-deoxyadenosyl radical that in turn initiates radical formation of substrate molecules or of glycyl residues within the target enzymes to activate them for radical-based chemistry. The source of the electron required for the cleavage of SAM is a reduced form of a conserved FeS cluster within the protein |
727079 |
| 4.1.99.22 | S-adenosyl-L-methionine |
the S-adenosyl-L-methionine-dependent enzyme MoaA, in concert with MoaC, catalyzes the first step of molybdenum cofactor biosynthesis, the conversion of 5'-GTP into precursor Z |
715257 |
