APOBEC

Example of a member of the APOBEC family, APOBEC-2. A cytidine deaminase from Homo sapiens.^[1]

APOBEC-like N-terminal domain

Identifiers

Symbol

APOBEC_N

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

APOBEC-like C-terminal domain

Identifiers

Symbol

APOBEC_C

Available protein structures:
Pfam	structures
PDB	RCSB PDB; PDBe; PDBj
PDBsum	structure summary

APOBEC ("apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like") is a family of evolutionarily conserved proteins.

A mechanism of generating protein diversity is mRNA editing. Members of this family are C-to-U editing enzymes. The N-terminal domain of APOBEC like proteins is the catalytic domain, while the C-terminal domain is a pseudocatalytic domain. More specifically, the catalytic domain is a zinc dependent cytidine deaminase domain and is essential for cytidine deamination. RNA editing by APOBEC-1 requires homodimerisation and this complex interacts with RNA binding proteins to form the editosome.^[2] A recent review discussed the structural and biophysical aspects of APOBEC3 family enzymes.^[3] Much of the APOBEC protein features are described in the widely studied APOBEC3G's page.

Family members

Human genes encoding members of the APOBEC protein family include:

APOBEC1
APOBEC2
APOBEC3A
APOBEC3B
APOBEC3C
APOBEC3D ("APOBEC3E" now refers to this)
APOBEC3F
APOBEC3G
APOBEC3H
APOBEC4
Activation-induced (cytidine) deaminase

References

↑ PDB: 2NYT; Prochnow, C.; Bransteitter, R.; Klein, M.G.; Goodman, M.F.; Chen, X.S.; functional implications for the deaminase AID. (2007). "The APOBEC-2 crystal structure". Nature. 445 (7126): 447–451. doi:10.1038/nature05492. PMID 17187054. ; rendered using PyMOL.
↑ Wedekind JE, Dance GS, Sowden MP, Smith HC (April 2003). "Messenger RNA editing in mammals: new members of the APOBEC family seeking roles in the family business". Trends Genet. 19 (4): 207–16. doi:10.1016/S0168-9525(03)00054-4. PMID 12683974.
↑ Jaguva Vasudevan, AA; Smits SH; Höppner A; Häussinger D; Koenig BW; Münk C. (June 2013). "Structural features of antiviral DNA cytidine deaminases". Biol Chem. 394 (11): 1357–1370. doi:10.1515/hsz-2013-0165. PMID 23787464.

This article incorporates text from the public domain Pfam and InterPro IPR013158

Hydrolases: carbon-nitrogen non-peptide (EC 3.5)

3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aspartoacylase Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin

3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase

3.5.3: Linear amidines/ Ureohydrolases	Arginase Agmatinase Protein-arginine deiminase

3.5.4: Cyclic amidines/ Aminohydrolases	Guanine deaminase Adenosine deaminase AMP deaminase Inosine monophosphate synthase DCMP deaminase GTP cyclohydrolase I Cytidine deaminase AICDA Activation-induced cytidine deaminase

3.5.5: Nitriles/ Aminohydrolases	Nitrilase

3.5.99: Other	Riboflavinase Thiaminase II

Enzymes

Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Catalytically perfect enzyme Coenzyme Cofactor Enzyme catalysis Enzyme kinetics Lineweaver–Burk plot Michaelis–Menten kinetics

Regulation	Allosteric regulation Cooperativity Enzyme inhibitor

Classification	EC number Enzyme superfamily Enzyme family List of enzymes

Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list)

This article is issued from Wikipedia - version of the 5/16/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.