Streptothricin hydrolase

Last updated
Streptothricin hydrolase
Identifiers
EC no. 3.5.2.19
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Search
PMC articles
PubMed articles
NCBI proteins

Streptothricin hydrolase (EC 3.5.2.19, sttH (gene)) is an enzyme with systematic name streptothricin-F hydrolase. [1] [2] This enzyme catalyses the following chemical reaction

streptothricin-F + H2O streptothricin-F acid

The enzyme also catalyses the hydrolysis of streptothricin-D to streptothricin-D acid.

Related Research Articles

β-Amylase Enzyme that hydrolyses alpha-1,4-D-glucosidic bonds in polysaccharides

β-Amylase is an enzyme with the systematic name 4-α-D-glucan maltohydrolase. It catalyses the following reaction:

<span class="mw-page-title-main">Fumarylacetoacetate hydrolase</span>

Fumarylacetoacetase is an enzyme that in humans is encoded by the FAH gene located on chromosome 15. The FAH gene is thought to be involved in the catabolism of the amino acid phenylalanine in humans.

The crotonase family comprises mechanistically diverse proteins that share a conserved trimeric quaternary structure, the core of which consists of 4 turns of a (beta/beta/alpha)n superhelix.

Glucan 1,4-α-glucosidase Enzyme that hydrolyses terminal α-1,4-D-glucose residues of polysaccharides

Glucan 1,4-α-glucosidase is an enzyme located on the brush border of the small intestine with systematic name 4-α-D-glucan glucohydrolase. It catalyses the following chemical reaction

<span class="mw-page-title-main">Microsomal epoxide hydrolase</span>

In enzymology, a microsomal epoxide hydrolase (mEH) is an enzyme that catalyzes the hydrolysis reaction between an epoxide and water to form a diol.

A ureohydrolase is a type of hydrolase enzyme. The ureohydrolase superfamily includes arginase, agmatinase, formiminoglutamase and proclavaminate amidinohydrolase. These enzymes share a 3-layer alpha-beta-alpha structure, and play important roles in arginine/agmatine metabolism, the urea cycle, histidine degradation, and other pathways.

In molecular biology, glycoside hydrolase family 15 is a family of glycoside hydrolases.

<span class="mw-page-title-main">Haloacid dehydrogenase superfamily</span>

The haloacid dehydrogenase superfamily is a superfamily of enzymes that include phosphatases, phosphonatases, P-type ATPases, beta-phosphoglucomutases, phosphomannomutases, and dehalogenases, and are involved in a variety of cellular processes ranging from amino acid biosynthesis to detoxification.

Enzyme promiscuity is the ability of an enzyme to catalyse a fortuitous side reaction in addition to its main reaction. Although enzymes are remarkably specific catalysts, they can often perform side reactions in addition to their main, native catalytic activity. These promiscuous activities are usually slow relative to the main activity and are under neutral selection. Despite ordinarily being physiologically irrelevant, under new selective pressures these activities may confer a fitness benefit therefore prompting the evolution of the formerly promiscuous activity to become the new main activity. An example of this is the atrazine chlorohydrolase from Pseudomonas sp. ADP that evolved from melamine deaminase, which has very small promiscuous activity toward atrazine, a man-made chemical.

Cannabidiolic acid synthase is an enzyme with systematic name cannabigerolate:oxygen oxidoreductase . It is an oxidoreductase found in Cannabis sativa that catalyses the formation of cannabidiolate, a carboxylated precursor of cannabidiol.

Endo-α-N-acetylgalactosaminidase (EC 3.2.1.97, endo-α-acetylgalactosaminidase, endo-α-N-acetyl-D-galactosaminidase, mucinaminylserine mucinaminidase, D-galactosyl-3-(N-acetyl-α-D-galactosaminyl)-L-serine mucinaminohydrolase, endo-α-GalNAc-ase, D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase) is an enzyme with systematic name glycopeptide-D-galactosyl-N-acetyl-α-D-galactosamine D-galactosyl-N-acetyl-galactosaminohydrolase. This enzyme catalyses the following chemical reaction

Beta-D-glucopyranosyl abscisate beta-glucosidase (EC 3.2.1.175, AtBG1, ABA-beta-D-glucosidase, ABA-specific beta-glucosidase, ABA-GE hydrolase, beta-D-glucopyranosyl abscisate hydrolase) is an enzyme with systematic name beta-D-glucopyranosyl abscisate glucohydrolase. This enzyme catalyses the following chemical reaction

Gellan tetrasaccharide unsaturated glucuronyl hydrolase (EC 3.2.1.179, UGL, unsaturated glucuronyl hydrolase) is an enzyme with systematic name beta-D-4-deoxy-Delta4-GlcAp-(1->4)-beta-D-Glcp-(1->4)-alpha-L-Rhap-(1->3)-beta-D-Glcp beta-D-4-deoxy-Delta4-GlcAp hydrolase. This enzyme catalyses the following chemical reaction

Acylaminoacyl-peptidase is an enzyme. This enzyme catalyses the following chemical reaction

<span class="mw-page-title-main">Gamma-glutamyl hydrolase</span> Protein-coding gene in the species Homo sapiens

Ghk.

UDP-2,4-diacetamido-2,4,6-trideoxy-beta-L-altropyranose hydrolase (EC 3.6.1.57, PseG, UDP-6-deoxy-AltdiNAc hydrolase, Cj1312) is an enzyme with systematic name UDP-2,4-bis(acetamido)-2,4,6-trideoxy-beta-L-altropyranose hydrolase. This enzyme catalyses the following chemical reaction

4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase (EC 3.7.1.17, tesD (gene), hsaD (gene)) is an enzyme with systematic name 4,5:9,10-diseco-3-hydroxy-5,9,17-trioxoandrosta-1(10),2-diene-4-oate hydrolase ( (2Z,4Z)-2-hydroxyhexa-2,4-dienoate-forming). This enzyme catalyses the following chemical reaction

6-oxocamphor hydrolase (EC 3.7.1.18, OCH, camK (gene)) is an enzyme with systematic name bornane-2,6-dione hydrolase. This enzyme catalyses the following chemical reaction

Terpentetriene synthase is an enzyme with systematic name terpentedienyl-diphosphate diphosphate-lyase (terpentetriene-forming). This enzyme catalyses the following chemical reaction

Terpentedienyl-diphosphate synthase is an enzyme with systematic name terpentedienyl-diphosphate lyase (decyclizing). This enzyme catalyses the following chemical reaction

References

  1. Maruyama C, Hamano Y (November 2009). "The biological function of the bacterial isochorismatase-like hydrolase SttH". Bioscience, Biotechnology, and Biochemistry. 73 (11): 2494–500. doi: 10.1271/bbb.90499 . PMID   19897889.
  2. Hamano Y, Matsuura N, Kitamura M, Takagi H (June 2006). "A novel enzyme conferring streptothricin resistance alters the toxicity of streptothricin D from broad-spectrum to bacteria-specific". The Journal of Biological Chemistry. 281 (25): 16842–8. doi: 10.1074/jbc.m602294200 . PMID   16641084.