| 8-oxoguanine deaminase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.5.4.32 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
8-oxoguanine deaminase (EC 3.5.4.32, 8-OGD) is an enzyme with systematic name 8-oxoguanine aminohydrolase. [1] This enzyme catalyses the following chemical reaction
Zn2+ is bound in the active site.
Adenosine deaminase is an enzyme involved in purine metabolism. It is needed for the breakdown of adenosine from food and for the turnover of nucleic acids in tissues.
OGD may refer to:
8-Oxoguanine glycosylase, also known as OGG1, is a DNA glycosylase enzyme that, in humans, is encoded by the OGG1 gene. It is involved in base excision repair. It is found in bacterial, archaeal and eukaryotic species.
Atrazine Chlorohydrolase (AtzA) is an enzyme (E.C.3.8.1.8), which catalyzes the conversion of atrazine to hydroxyatrazine. Bacterial degradation determines the environmental impact and efficacy of an herbicide or pesticide. Initially, most pesticides are highly effective and show minimal bacterial degradation; however, bacteria can rapidly evolve and gain the ability to metabolize potential nutrients in the environment. Despite a remarkable structural similarity, degradation of atrazine by bacteria capable of melamine degradation was rare; however, since its introduction as a pesticide in the United States, bacteria capable of atrazine degradation have evolved. Currently, Pseudomonas sp. strain ADP seems to be the optimal bacterial strain for atrazine degradations, which appears to be the sole nitrogen source for the bacteria.
dCMP deaminase is an enzyme which converts deoxycytidylic acid to deoxyuridylic acid.
The enzyme ethanolamine ammonia-lyase (EC 4.3.1.7) catalyzes the chemical reaction
The enzyme L-serine ammonia-lyase (EC 4.3.1.17) catalyzes the chemical reaction
In enzymology, an adenosine-phosphate deaminase (EC 3.5.4.17) is an enzyme that catalyzes the chemical reaction
In enzymology, an ADP deaminase (EC 3.5.4.7) is an enzyme that catalyzes the chemical reaction
In enzymology, a cytosine deaminase (EC 3.5.4.1) is an enzyme that catalyzes the chemical reaction
In enzymology, a dCTP deaminase (EC 3.5.4.13) is an enzyme that catalyzes the chemical reaction
In enzymology, a deoxycytidine deaminase (EC 3.5.4.5) is an enzyme that catalyzes the chemical reaction
In enzymology, a pterin deaminase (EC 3.5.4.11) is an enzyme that catalyzes the chemical reaction
In enzymology, a sepiapterin deaminase (EC 3.5.4.24) is an enzyme that catalyzes the chemical reaction
Cytidine deaminase is an enzyme that in humans is encoded by the CDA gene.
8-Oxoguanine (8-hydroxyguanine, 8-oxo-Gua, or OH8Gua) is one of the most common DNA lesions resulting from reactive oxygen species modifying guanine, and can result in a mismatched pairing with adenine resulting in G to T and C to A substitutions in the genome. In humans, it is primarily repaired by DNA glycosylase OGG1. It can be caused by ionizing radiation, in connection with oxidative metabolism.
S-methyl-5'-thioadenosine deaminase (EC 3.5.4.31, MTA deaminase, 5-methylthioadenosine deaminase) is an enzyme with systematic name S-methyl-5'-thioadenosine amidohydrolase. This enzyme catalyses the following chemical reaction
8-oxo-dGTP diphosphatase (EC 3.6.1.55, MutT, 7,8-dihydro-8-oxoguanine triphosphatase, 8-oxo-dGTPase, 7,8-dihydro-8-oxo-dGTP pyrophosphohydrolase) is an enzyme with systematic name 8-oxo-dGTP diphosphohydrolase. This enzyme catalyses the following chemical reaction:
The enzyme 3,4-dihydroxyphenylalanine reductive deaminase (EC 4.3.1.22, reductive deaminase, DOPA-reductive deaminase, DOPARDA; systematic name 3,4-dihydroxy-L-phenylalanine ammonia-lyase (3,4-dihydroxyphenylpropanoate-forming)) catalyses the following chemical reaction
Mutational signatures are characteristic combinations of mutation types arising from specific mutagenesis processes such as DNA replication infidelity, exogenous and endogenous genotoxin exposures, defective DNA repair pathways, and DNA enzymatic editing.
