Health Topics
Official websites use .gov
A
.gov website belongs to an official government
organization in the United States.
Secure .gov websites use HTTPS
A
lock (
) or https:// means you’ve safely connected to
the .gov website. Share sensitive information only on official,
secure websites.
Normal Function
The FTCD gene provides instructions for making an enzyme called formimidoyltransferase-cyclodeaminase. This enzyme is found mainly in the liver, although small amounts are found in the kidneys and the testes. Formimidoyltransferase-cyclodeaminase is called a bifunctional enzyme because it performs two functions.
The first function of formimidoyltransferase-cyclodeaminase is to act as a transferase, which is an enzyme that moves (transfers) a group of atoms from one molecule to another. By doing this, the enzyme converts formiminoglutamate (FIGLU) to 5-formiminotetrahydrofolate. The amino acid glutamate, which is a building block of many proteins, is also produced during this process.
Formimidoyltransferase-cyclodeaminase also acts as a deaminase, which is an enzyme that removes a group of nitrogen and hydrogen atoms from other molecules. By doing this, the enzyme converts 5-formiminotetrahydrofolate to a different tetrahydrofolate molecule. Tetrahydrofolate molecules are involved in producing purines and pyrimidines, which are the building blocks of DNA and its chemical cousin, RNA. The tetrahydrofolates carry small molecules called one-carbon units that are needed to produce these larger molecules.
These two functions make up the final two steps in the breakdown of the amino acid histidine.
Health Conditions Related to Genetic Changes
Glutamate formiminotransferase deficiency
Variants (also called mutations) in the FTCD gene cause glutamate formiminotransferase deficiency, an inherited disorder that can result in high levels of FIGLU in the urine. In the past, researchers recognized a mild form and a severe form of this condition. However, some people with glutamate formiminotransferase deficiency do not appear to have any related health problems.
The FTCD gene variants that cause glutamate formiminotransferase deficiency alter the function of formimidoyltransferase-cyclodeaminase, which disrupts the enzyme’s ability to completely break down histidine. If the enzyme’s transferase activity is impaired, FIGLU can build up in the body and then be released in the urine. It is unclear exactly how these changes are related to the specific health problems seen in some people with glutamate formiminotransferase deficiency.
More About This Health ConditionOther Names for This Gene
- formiminotransferase cyclodeaminase
- LCHC1
Additional Information & Resources
Tests Listed in the Genetic Testing Registry
Scientific Articles on PubMed
Catalog of Genes and Diseases from OMIM
References
- Ahrens-Nicklas RC, Ganetzky RD, Rush PW, Conway RL, Ficicioglu C. Characteristics and outcomes of patients with formiminoglutamic aciduria detected through newborn screening. J Inherit Metab Dis. 2019 Jan;42(1):140-146. doi: 10.1002/jimd.12035. Citation on PubMed
- Hilton JF, Christensen KE, Watkins D, Raby BA, Renaud Y, de la Luna S, Estivill X, MacKenzie RE, Hudson TJ, Rosenblatt DS. The molecular basis of glutamate formiminotransferase deficiency. Hum Mutat. 2003 Jul;22(1):67-73. doi: 10.1002/humu.10236. Citation on PubMed
- Mao Y, Vyas NK, Vyas MN, Chen DH, Ludtke SJ, Chiu W, Quiocho FA. Structure of the bifunctional and Golgi-associated formiminotransferase cyclodeaminase octamer. EMBO J. 2004 Aug 4;23(15):2963-71. doi: 10.1038/sj.emboj.7600327. Epub 2004 Jul 22. Citation on PubMed or Free article on PubMed Central
- Niederwieser A, Giliberti P, Matasovic A, Pluznik S, Steinmann B, Baerlocher K. Folic acid non-dependent formiminoglutamic aciduria in two siblings. Clin Chim Acta. 1974 Aug 20;54(3):293-316. doi: 10.1016/0009-8981(74)90248-4. No abstract available. Citation on PubMed
- Solans A, Estivill X, de la Luna S. Cloning and characterization of human FTCD on 21q22.3, a candidate gene for glutamate formiminotransferase deficiency. Cytogenet Cell Genet. 2000;88(1-2):43-9. doi: 10.1159/000015483. Citation on PubMed
The information on this site should not be used as a substitute for professional medical care or advice. Contact a health care provider if you have questions about your health.