Protein Family Models

Domain II of the enzyme dihydroprymidine dehydrogenase binds FAD. Dihydroprymidine dehydrogenase catalyses the first and rate-limiting step of pyrimidine degradation by converting pyrimidines to the corresponding 5,6- dihydro compounds [1]. This domain carries two Fe4-S4 clusters. [1]. 11796730. Crystal structure of the productive ternary complex of. dihydropyrimidine dehydrogenase with NADPH and 5-iodouracil.. Implications for mechanism of inhibition and electron transfer.. Dobritzsch D, Ricagno S, Schneider G, Schnackerz KD, Lindqvist. Y;. J Biol Chem. 2002;277:13155-13166. (from Pfam)

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2024-08-14

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2024-08-14

This family of proteins contains FAD dependent oxidoreductases and related proteins. (from Pfam)

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2024-08-14

This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase. multienzyme complex: dihydrolipoamide dehydrogenase complexed. with the binding domain of dihydrolipoamide acetyltransferase.. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)

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2024-08-14

This family consists of various amine oxidases, including maze polyamine oxidase (PAO) [1] and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines [2]. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium [3]. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines [1]. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins. [1]. 9598979. Maize polyamine oxidase: primary structure from protein and cDNA. sequencing.. Tavladoraki P, Schinina ME, Cecconi F, Agostino SD, Manera F,. Rea G, Mariottini P, Federico R, Angelini R;. FEBS Lett 1998;426:62-66.. [2]. 9162023. A key amino acid responsible for substrate selectivity of. monoamine oxidase A and B.. Tsugeno Y, Ito A;. J Biol Chem 1997;272:14033-14036.. [3]. 7770050. Cloning, sequencing and heterologous expression of the monoamine. oxidase gene from Aspergillus niger.. Schilling B, Lerch K;. Mol Gen Genet 1995;247:430-438. (from Pfam)

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2024-08-14

This domain is involved in FAD binding in a number of enzymes. [1]. 1409567. Crystal structure of the reduced form of p-hydroxybenzoate. hydroxylase refined at 2.3A resolution.. Schreuder HA, van der Laan JM, Swarte MB, Kalk KH, Hol WG,. Drenth J;. Proteins 1992;14:178-190. (from Pfam)

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2024-08-14

This family includes members that bind FAD. This family includes the flavoprotein subunits from succinate and fumarate dehydrogenase, aspartate oxidase and the alpha subunit of adenylylsulphate reductase. [1]. 8061609. Structure of glutathione reductase from Escherichia coli at 1.86. A resolution: comparison with the enzyme from human. erythrocytes.. Mittl PR, Schulz GE. Protein Sci 1994;3:799-809. (from Pfam)

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2024-08-14

This family includes both class I and class II oxidoreductases and also NADH oxidases and peroxidases. This domain is actually a small NADH binding domain within a larger FAD binding domain. [1]. 8805537. Protein-protein interactions in the pyruvate dehydrogenase. multienzyme complex: dihydrolipoamide dehydrogenase complexed. with the binding domain of dihydrolipoamide acetyltransferase.. Mande SS, Sarfaty S, Allen MD, Perham RN, Hol WG;. Structure 1996;4:277-286. (from Pfam)

Date:

2024-08-14