DCMP deaminase

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dCMP deaminase
dCMP deaminase
	Deoxycytidylate deaminase hexamer, Cyanophage s-tim5
Identifiers
EC no.	3.5.4.12
CAS no.	9026-92-0
Databases
BRENDA	enzyme data
ExPASy	NiceZyme view
KEGG	enzyme entry
MetaCyc	metabolic pathway
Rhea	reactions
PDB structures	RCSB PDB PDBe PDBsum
Gene Ontology	AmiGO / QuickGO
PMC
Search
PMC	articles
PubMed	articles
NCBI	proteins

DCTD
Identifiers
Aliases	DCTD, dCMP deaminase
External IDs	OMIM: 607638; MGI: 2444529; GeneCards: DCTD
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	2W4L
Enzyme activity
Gene location (Human)
Chr.	Chromosome 4 (human)
End	182,917,936 bp
Gene location (Mouse)
Chr.	Chromosome 8 (mouse)
End	48,606,268 bp
RNA expression pattern
	Top expressed in
	stromal cell of endometrium; ; right adrenal gland; ; left adrenal gland; ; gallbladder; ; right adrenal cortex; ; islet of Langerhans; ; left adrenal cortex; ; left lobe of thyroid gland; ; right lobe of thyroid gland; ; canal of the cervix;
	Top expressed in
	genital tubercle; ; tail of embryo; ; zygote; ; hand; ; secondary oocyte; ; epiblast; ; morula; ; embryo; ; embryo; ; primitive streak;
	More reference expression data
	n/a
Gene ontology
Molecular function	zinc ion binding; catalytic activity; hydrolase activity; protein binding; metal ion binding; identical protein binding; dCMP deaminase activity;
Cellular component	cytosol; cytoplasm;
Biological process	pyrimidine nucleotide metabolic process; metabolism; nucleotide biosynthetic process; nucleobase-containing small molecule interconversion; dUMP biosynthetic process; dTMP biosynthetic process;
	Sources:Amigo / QuickGO
Orthologs
Databases	NCBI: entry; OMA: entry
	1635
	320685
	ENSG00000129187
	ENSMUSG00000031562
	P32321
	Q8K2D6
NM_001012732; NM_001921; NM_001351743; NM_001351744; NM_001351745;
	NM_001351747; NM_001351748; NM_001351750; NM_001351753
	NM_001161515; NM_001161516; NM_178788
NP_001012750; NP_001912; NP_001338672; NP_001338673; NP_001338674;
	NP_001338676; NP_001338677; NP_001338679; NP_001338682
	NP_001154987; NP_001154988; NP_848903
	Wikidata
View/Edit Human	View/Edit Mouse

dCMP deaminase

Identifiers

Symbol

DCTD

Other data

Chr. 4 q35.1

Search for
Structures	Swiss-model
Domains	InterPro

dCMP deaminase (EC 3.5.4.12) is an enzyme which in humans is encoded by the gene DCTD. The name refers to its enzymatic activity which converts deoxycytidine monophosphate to deoxyuridine monophosphate and ammonia. Alternate names for the enzyme include deoxycytidylate deaminase, deoxy-CMP-deaminase, deoxycytidylate aminohydrolase, deoxycytidine monophosphate deaminase, and deoxycytidine-5'-phosphate deaminase, deoxycytidine-5'-monophosphate aminohydrolase.

deoxycytidine monophosphate

H₂O

NH₃

Rightward reaction arrow with minor substrate(s) from top left and minor product(s) to top right

deoxyuridine monophosphate

The enzyme is part of the metabolic pathway for pyrimidines. A modified version has been used in a production system for uridine monophosphate.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000129187 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031562 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Enzyme 3.5.4.12 at KEGG Pathway Database.
↑ Scarano E (March 1960). "The enzymatic deamination of 6-aminopyrimidine deoxyribonucleotides. I. The enzymatic deamination of deoxycytidine 5'-phosphate and of 5-methyldeoxycytidine 5-methyldeoxycytidine 5'-phosphate". The Journal of Biological Chemistry. 235 (3): 706–713. doi:10.1016/S0021-9258(19)67927-5. PMID 14442222.
↑ Scarano E, Bonaduce L (December 1960). "The enzymatic deamination of 6-aminopyrimidine deoxyribonucleotides. II. Purification and properties of a 6-aminopyrimidine deoxyribonucleoside 5'-phosphate deaminase from unfertilized eggs of sea urchine". The Journal of Biological Chemistry. 235 (12): 3556–3561. doi:10.1016/S0021-9258(18)64507-7. PMID 13747062.
↑ Sergott RC, Debeer LJ, Bessman MJ (December 1971). "On the regulation of a bacterial deoxycytidylate deaminase". The Journal of Biological Chemistry. 246 (24): 7755–7758. doi:10.1016/S0021-9258(19)45839-0. PMID 5002683.
↑ Ligasová A, Horejšová M, Brumarová R, Friedecký D, Koberna K (August 2025). "Cytidine and dCMP Deaminases-Current Methods of Activity Analysis". International Journal of Molecular Sciences. 26 (16): 8045. doi:10.3390/ijms26168045. PMC 12386326. PMID 40869362.
↑ Li ZL, Chen T, Li ZM (November 2025). "Engineering the Activity and Stability of dCMP Deaminase To Achieve Efficient and Simple Production of Uridine Monophosphate". Journal of Agricultural and Food Chemistry. 73 (46): 29674–29682. doi:10.1021/acs.jafc.5c07607. PMID 41196667.

External links

dCMP+deaminase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000129187 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000031562 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[5] Enzyme 3.5.4.12 at KEGG Pathway Database.

[6] Scarano E (March 1960). "The enzymatic deamination of 6-aminopyrimidine deoxyribonucleotides. I. The enzymatic deamination of deoxycytidine 5'-phosphate and of 5-methyldeoxycytidine 5-methyldeoxycytidine 5'-phosphate". The Journal of Biological Chemistry. 235 (3): 706–713. doi:10.1016/S0021-9258(19)67927-5. PMID 14442222.

[7] Scarano E, Bonaduce L (December 1960). "The enzymatic deamination of 6-aminopyrimidine deoxyribonucleotides. II. Purification and properties of a 6-aminopyrimidine deoxyribonucleoside 5'-phosphate deaminase from unfertilized eggs of sea urchine". The Journal of Biological Chemistry. 235 (12): 3556–3561. doi:10.1016/S0021-9258(18)64507-7. PMID 13747062.

[8] Sergott RC, Debeer LJ, Bessman MJ (December 1971). "On the regulation of a bacterial deoxycytidylate deaminase". The Journal of Biological Chemistry. 246 (24): 7755–7758. doi:10.1016/S0021-9258(19)45839-0. PMID 5002683.

[9] Ligasová A, Horejšová M, Brumarová R, Friedecký D, Koberna K (August 2025). "Cytidine and dCMP Deaminases-Current Methods of Activity Analysis". International Journal of Molecular Sciences. 26 (16): 8045. doi:10.3390/ijms26168045. PMC 12386326. PMID 40869362.

[10] Li ZL, Chen T, Li ZM (November 2025). "Engineering the Activity and Stability of dCMP Deaminase To Achieve Efficient and Simple Production of Uridine Monophosphate". Journal of Agricultural and Food Chemistry. 73 (46): 29674–29682. doi:10.1021/acs.jafc.5c07607. PMID 41196667.

v t e Hydrolases: carbon-nitrogen non-peptide (EC 3.5)
3.5.1: Linear amides / Amidohydrolases	Asparaginase Glutaminase Urease Biotinidase Aminoacylase ACY1 Aspartoacylase(ACY2) ACY3 Ceramidase Aspartylglucosaminidase Fatty acid amide hydrolase Histone deacetylase Sirtuin
3.5.2: Cyclic amides/ Amidohydrolases	Barbiturase Beta-lactamase Dihydroorotase
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

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)