Protein Family Models

Cyanate hydratase (also known as cyanate lyase) catalyses the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide, allowing the host organisms to overcome the toxicity of environmental cyanate [1-4]. It consists of an N-terminal five-helix bundle domain that shows structural similarity to DNA-binding HTH domains and a C-terminal catalytic domain, which has a unique fold [4]. Paper describing PDB structure 1dw9. [1]. 10801492. Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site. Walsh MA, Otwinowski Z, Perrakis A, Anderson PM, Joachimiak A;. Structure Fold Des 2000;8:505-514. Paper describing PDB structure 4y42. [2]. 25849512. Serendipitous crystallization and structure determination of cyanase (CynS) from Serratia proteamaculans. Butryn A, Stoehr G, Linke-Winnebeck C, Hopfner KP;. Acta Crystallogr F Struct Biol Commun. 2015;71:471-476. Paper describing PDB structure 5uk3. [3]. 28613863. Structural Characterization of a Eukaryotic Cyanase from Tetranychus urticae. Schlachter CR, Klapper V, Wybouw N, Radford T, Van Leeuwen T, Grbic M, Chruszcz M;. J Agric Food Chem. 2017;65:5453-5462. Paper describing PDB structure 6tv0. [4]. 32880586. Detecting the nature and solving the crystal structure of a contaminant protein from an opportunistic pathogen. Pederzoli R, Tarantino D, Gourlay LJ, Chaves-Sanjuan A, Bolognesi M;. Acta Crystallogr F Struct Biol Commun. 2020;76:392-397. (from Pfam)

Date:

2024-10-16

Cyanate lyase (also known as cyanase) EC:4.2.1.104 is responsible for the hydrolysis of cyanate, allowing organisms that possess the enzyme to overcome the toxicity of environmental cyanate. This enzyme is composed of two domains, an N-terminal helix-turn-helix and this structurally unique C-terminal domain [2]. [1]. 3049588. Characterization of the cyn operon in Escherichia coli K12. Sung YC, Fuchs JA;. J Biol Chem 1988;263:14769-14775. [2]. 10801492. Structure of cyanase reveals that a novel dimeric and decameric arrangement of subunits is required for formation of the enzyme active site. Walsh MA, Otwinowski Z, Perrakis A, Anderson PM, Joachimiak A;. Structure Fold Des 2000;8:505-514. (from Pfam)

Date:

2024-10-16

cyanase catalyzes the reaction of cyanate with bicarbonate to produce ammonia and carbon dioxide, and is used to decompose cyanate for use as the sole source of nitrogen

Date:

2018-03-22

Catalyzes the reaction of cyanate and bicarbonate to produce ammonia and carbon dioxide

Date:

2020-10-26

Alternate names include cyanate C-N-lyase, cyanate hydratase, and cyanate hydrolase.

Gene:

cynS

Date:

2024-06-11