ALDH4A1
ALDH4A1 (aldehyde dehydrogenase 4 family member A1, also known as P5CDh or ALDH4) is a mitochondrial matrix NAD-dependent dehydrogenase. It converts delta-1-pyrroline-5-carboxylate to glutamate in the proline degradation pathway. Browse Assay Genie's current range of ALDH4A1 research reagents below, or read on for the biology behind the target.
ALDH4A1 catalyses the irreversible conversion of delta-1-pyrroline-5-carboxylate (P5C), derived from either proline or ornithine, to glutamate. This is the second step of the proline degradation pathway and a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles. The enzyme depends on NAD. Its preferred substrate is glutamic gamma-semialdehyde, and it can also act on succinic, glutaric and adipic semialdehydes.
The ALDH4A1 protein is found in the mitochondrial matrix and belongs to the aldehyde dehydrogenase family. In the HGNC classification the gene sits in the aldehyde dehydrogenases group, and it is also listed among microRNA protein coding host genes. The human ALDH4A1 gene has orthologues in mouse and rat, both named Aldh4a1. According to the NCBI Gene summary, alternatively spliced transcript variants encoding different isoforms have been identified.
The enzyme is also known as delta-1-pyrroline-5-carboxylate dehydrogenase (P5CDh), and the gene was previously named aldehyde dehydrogenase 4 family, member A1. Deficiency of the enzyme is associated with type II hyperprolinemia, an autosomal recessive disorder characterised by accumulation of P5C and proline. This makes ALDH4A1 a useful reference point for work on proline catabolism and mitochondrial amino acid metabolism, and for comparison with other aldehyde dehydrogenase family members.
ALDH4A1 catalyses the second step of proline degradation, converting pyrroline-5-carboxylate to glutamate, so it is central to studies of proline catabolism.
The enzyme carries out a necessary step in the pathway interconnecting the urea and tricarboxylic acid cycles, with P5C derived from proline or ornithine.
Deficiency of ALDH4A1 is associated with type II hyperprolinemia, an autosomal recessive disorder marked by accumulation of P5C and proline.
As a mitochondrial member of the aldehyde dehydrogenase family with semialdehyde substrates, ALDH4A1 supports comparative studies of substrate preference across the family.
ALDH4A1 irreversibly converts delta-1-pyrroline-5-carboxylate, derived from proline or ornithine, to glutamate in the mitochondrial matrix. It uses NAD, acts in the second step of proline degradation, and contributes to the pathway linking the urea and tricarboxylic acid cycles.
ALDH4A1 is also called P5CDh and ALDH4, and its UniProt name is delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial. Its earlier gene name was aldehyde dehydrogenase 4 family, member A1. NCBI Gene reports alternatively spliced transcript variants that encode different isoforms.
Deficiency of ALDH4A1 is associated with type II hyperprolinemia, an autosomal recessive disorder in which P5C and proline accumulate. The gene has orthologues named Aldh4a1 in mouse and rat; check the datasheet of any product for its validated reactivity.
Other aldehyde dehydrogenase family members and related metabolic enzymes with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P30038; product specifications from Assay Genie datasheets.