Short-chain dehydrogenase

Last updated
short chain dehydrogenase
PDB 1hdc EBI.jpg
[1]
Identifiers
Symboladh_short
Pfam PF00106
InterPro IPR002198
PROSITE PDOC00060
SCOP2 1hdc / SCOPe / SUPFAM
OPM superfamily 119
OPM protein 1xu7
CDD cd02266
Membranome 246

The short-chain dehydrogenases/reductases family (SDR) [2] is a very large family of enzymes, most of which are known to be NAD- or NADP-dependent oxidoreductases. As the first member of this family to be characterised was Drosophila alcohol dehydrogenase, this family used to be called [3] [4] [5] 'insect-type', or 'short-chain' alcohol dehydrogenases. Most members of this family are proteins of about 250 to 300 amino acid residues. Most dehydrogenases possess at least 2 domains, [6] the first binding the coenzyme, often NAD, and the second binding the substrate. This latter domain determines the substrate specificity and contains amino acids involved in catalysis. Little sequence similarity has been found in the coenzyme binding domain although there is a large degree of structural similarity, and it has therefore been suggested that the structure of dehydrogenases has arisen through gene fusion of a common ancestral coenzyme nucleotide sequence with various substrate specific domains. [6]

Contents

Subfamilies

Human proteins containing this domain

BDH1; BDH2; CBR1; CBR3; CBR4; DCXR; DECR1; DECR2; DHRS1; DHRS10; DHRS13; DHRS2; DHRS3; DHRS4; DHRS4L2; DHRS7; DHRS7B; DHRS8; DHRS9; DHRSX; FASN; FVT1; HADH2; HPGD; HSD11B1; HSD11B2; HSD17B1; HSD17B10; HSD17B12; HSD17B13; HSD17B2; HSD17B3; HSD17B4; HSD17B6; HSD17B7; HSD17B7P2; HSD17B8; HSDL1; HSDL2; PECR; QDPR; RDH10; RDH11; RDH12; RDH13; RDH14; RDH16; RDH5; RDH8; RDHE2; RDHS; SCDR10; SPR; WWOX;

Related Research Articles

Alcohol dehydrogenase

Alcohol dehydrogenases (ADH) (EC 1.1.1.1) are a group of dehydrogenase enzymes that occur in many organisms and facilitate the interconversion between alcohols and aldehydes or ketones with the reduction of nicotinamide adenine dinucleotide (NAD+) to NADH. In humans and many other animals, they serve to break down alcohols that otherwise are toxic, and they also participate in generation of useful aldehyde, ketone, or alcohol groups during biosynthesis of various metabolites. In yeast, plants, and many bacteria, some alcohol dehydrogenases catalyze the opposite reaction as part of fermentation to ensure a constant supply of NAD+.

Acetaldehyde dehydrogenase

Acetaldehyde dehydrogenases are dehydrogenase enzymes which catalyze the conversion of acetaldehyde into acetic acid. The oxidation of acetaldehyde to acetate can be summarized as follows:

Methanofuran

Methanofurans are a family of chemical compounds found in methanogenic archaea. These species feature a 2-aminomethylfuran linked to phenoxy group. At least three different end groups are recognized: R = tricarboxyheptanoyl (methanofuran), glutamyl-glutamyl, tricarboxy-2-hydroxyheptanoyl.

17β-Hydroxysteroid dehydrogenases, also 17-ketosteroid reductases (17-KSR), are a group of alcohol oxidoreductases which catalyze the reduction of 17-ketosteroids and the dehydrogenation of 17β-hydroxysteroids in steroidogenesis and steroid metabolism. This includes interconversion of DHEA and androstenediol, androstenedione and testosterone, and estrone and estradiol.

In enzymology, a cinnamyl-alcohol dehydrogenase (EC 1.1.1.195) is an enzyme that catalyzes the chemical reaction

Homoserine dehydrogenase

In enzymology, a homoserine dehydrogenase (EC 1.1.1.3) is an enzyme that catalyzes the chemical reaction

3-Hydroxybutyryl-CoA dehydrogenase

In enzymology, a 3-hydroxybutyryl-CoA dehydrogenase (EC 1.1.1.157) is an enzyme that catalyzes the chemical reaction

Acyl-CoA dehydrogenase (NADP+)

In enzymology, an acyl-CoA dehydrogenase (NADP+) (EC 1.3.1.8) is an enzyme that catalyzes the chemical reaction

In enzymology, an alcohol dehydrogenase (acceptor) is an enzyme that catalyzes the chemical reaction

Guanylate kinase

In enzymology, a guanylate kinase is an enzyme that catalyzes the chemical reaction

Collagen, type VI, alpha 1

Collagen alpha-1(VI) chain is a protein that in humans is encoded by the COL6A1 gene.

HSD17B10

17-β-Hydroxysteroid dehydrogenase X (HSD10) also known as 3-hydroxyacyl-CoA dehydrogenase type-2 is a mitochondrial enzyme that in humans is encoded by the HSD17B10 gene. Several alternatively spliced transcript variants have been identified, but the full-length nature of only two transcript variants has been determined. Human HSD10 cDNA was cloned from brain (NM_004493), and the resulting protein, a homotetramer, was first characterized as a short chain 3-hydroxyacyl-CoA dehydrogenase (SCHAD). Active sites of this enzyme can accommodate different substrates; 17β-HSD10 is involved in the oxidation of isoleucine, branched-chain fatty acids, and xenobiotics as well as the metabolism of sex hormones and neuroactive steroids.

ADH4

Alcohol dehydrogenase 4 is an enzyme that in humans is encoded by the ADH4 gene.

SORD

Sorbitol dehydrogenase is an enzyme that in humans is encoded by the SORD gene.

HSD17B7

3-keto-steroid reductase is an enzyme that in humans is encoded by the HSD17B7 gene.

DHRS2

Dehydrogenase/reductase SDR family member 2 is an enzyme that in humans is encoded by the DHRS2 gene.

CBR3

Carbonyl reductase [NADPH] 3 is an enzyme that in humans is encoded by the CBR3 gene.

ELFV dehydrogenase

In molecular biology, the ELFV dehydrogenase family of enzymes include glutamate, leucine, phenylalanine and valine dehydrogenases. These enzymes are structurally and functionally related. They contain a Gly-rich region containing a conserved Lys residue, which has been implicated in the catalytic activity, in each case a reversible oxidative deamination reaction.

Group IV pyridoxal-dependent decarboxylases Family of enzymes

In molecular biology, group IV pyridoxal-dependent decarboxylases are a family of enzymes comprising ornithine decarboxylase EC 4.1.1.17, lysine decarboxylase EC 4.1.1.18, arginine decarboxylase EC 4.1.1.19 and diaminopimelate decarboxylaseEC 4.1.1.20. It is also known as the Orn/Lys/Arg decarboxylase class-II family.

Alcohol dehydrogenase (nicotinoprotein) is an enzyme with systematic name ethanol:acceptor oxidoreductase. This enzyme catalyses the following chemical reaction

References

  1. Ghosh D, Erman M, Wawrzak Z, Duax WL, Pangborn W (October 1994). "Mechanism of inhibition of 3 alpha, 20 beta-hydroxysteroid dehydrogenase by a licorice-derived steroidal inhibitor". Structure. 2 (10): 973–80. doi: 10.1016/S0969-2126(94)00099-9 . PMID   7866748.
  2. Persson B, Krook M, Atrian S, Gonzalez-Duarte R, Jeffery J, Ghosh D, Jornvall H (1995). "Short-chain dehydrogenases/reductases (SDR)". Biochemistry. 34 (18): 6003–6013. doi:10.1021/bi00039a038. PMID   7742302.
  3. Villarroya A, Juan E, Egestad B, Jornvall H (1989). "The primary structure of alcohol dehydrogenase from Drosophila lebanonensis. Extensive variation within insect 'short-chain' alcohol dehydrogenase lacking zinc". Eur. J. Biochem. 180 (1): 191–197. doi:10.1111/j.1432-1033.1989.tb14632.x. PMID   2707261.
  4. Persson B, Krook M, Jornvall H (1991). "Characteristics of short-chain alcohol dehydrogenases and related enzymes". Eur. J. Biochem. 200 (2): 537–543. doi:10.1111/j.1432-1033.1991.tb16215.x. PMID   1889416.
  5. Harayama S, Bairoch A, Hartnett C, Rekik M, Ornston LN, Neidle E (1992). "cis-diol dehydrogenases encoded by the TOL pWW0 plasmid xylL gene and the Acinetobacter calcoaceticus chromosomal benD gene are members of the short-chain alcohol dehydrogenase superfamily". Eur. J. Biochem. 204 (1): 113–120. doi:10.1111/j.1432-1033.1992.tb16612.x. PMID   1740120.
  6. 1 2 Benyajati C, Place AR, Powers DA, Sofer W (1981). "Alcohol dehydrogenase gene of Drosophila melanogaster: relationship of intervening sequences to functional domains in the protein". Proc. Natl. Acad. Sci. U.S.A. 78 (5): 2717–2721. Bibcode:1981PNAS...78.2717B. doi: 10.1073/pnas.78.5.2717 . PMC   319428 . PMID   6789320.