mimosinase | |||||||||
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Identifiers | |||||||||
EC no. | 3.5.1.61 | ||||||||
CAS no. | 104118-49-2 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a mimosinase (EC 3.5.1.61) is an enzyme that catalyzes the chemical reaction
Thus, the two substrates of this enzyme are (S)-2-amino-3-(3-hydroxy-4-oxo-4H-pyridin-1-yl)propanoate and H2O, whereas its two products are 3-hydroxy-4H-pyrid-4-one and L-serine.
This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is mimosine amidohydrolase.
Known to occur in all Leucaena and Mimosa . [1] Negi & Borthakur 2016 clone the synthase found in L. leucocephala . [1]
Heterologous expression in E. coli can be used. [1] Negi & Borthakur 2016 provide a protocol. [1]
Chymotrypsin (EC 3.4.21.1, chymotrypsins A and B, alpha-chymar ophth, avazyme, chymar, chymotest, enzeon, quimar, quimotrase, alpha-chymar, alpha-chymotrypsin A, alpha-chymotrypsin) is a digestive enzyme component of pancreatic juice acting in the duodenum, where it performs proteolysis, the breakdown of proteins and polypeptides. Chymotrypsin preferentially cleaves peptide amide bonds where the side chain of the amino acid N-terminal to the scissile amide bond (the P1 position) is a large hydrophobic amino acid (tyrosine, tryptophan, and phenylalanine). These amino acids contain an aromatic ring in their side chain that fits into a hydrophobic pocket (the S1 position) of the enzyme. It is activated in the presence of trypsin. The hydrophobic and shape complementarity between the peptide substrate P1 side chain and the enzyme S1 binding cavity accounts for the substrate specificity of this enzyme. Chymotrypsin also hydrolyzes other amide bonds in peptides at slower rates, particularly those containing leucine at the P1 position.
In molecular biology, biosynthesis is a multi-step, enzyme-catalyzed process where substrates are converted into more complex products in living organisms. In biosynthesis, simple compounds are modified, converted into other compounds, or joined to form macromolecules. This process often consists of metabolic pathways. Some of these biosynthetic pathways are located within a single cellular organelle, while others involve enzymes that are located within multiple cellular organelles. Examples of these biosynthetic pathways include the production of lipid membrane components and nucleotides. Biosynthesis is usually synonymous with anabolism.
Mimosine or leucenol is a toxic non-protein amino acid chemically similar to tyrosine. It occurs in some Mimosa spp. and all members of the closely related genus Leucaena.
In enzymology, a (S)-6-hydroxynicotine oxidase (EC 1.5.3.5) is an enzyme that catalyzes the chemical reaction
In enzymology, an aerobactin synthase (EC 6.3.2.39) is an enzyme that catalyzes the chemical reaction
The enzyme imidazoleglycerol-phosphate dehydratase (EC 4.2.1.19) catalyzes the chemical reaction
The enzyme pyrazolylalanine synthase (EC 4.2.1.50) catalyzes the chemical reaction
The enzyme 3-hydroxyisobutyryl-CoA hydrolase (EC 3.1.2.4) catalyzes the reaction
In enzymology, a diaminohydroxyphosphoribosylaminopyrimidine deaminase (EC 3.5.4.26) is an enzyme that catalyzes the chemical reaction
In enzymology, a hydroxyisourate hydrolase (EC 3.5.2.17) is an enzyme that catalyzes the chemical reaction
In enzymology, an imidazolonepropionase (EC 3.5.2.7) is an enzyme that catalyzes the chemical reaction
In enzymology, a beta-pyrazolylalanine synthase (EC 2.5.1.51) is an enzyme that catalyzes the chemical reaction
In enzymology, a L-mimosine synthase (EC 2.5.1.52) is an enzyme that catalyzes the chemical reaction
3-Succinoylsemialdehyde-pyridine dehydrogenase (EC 1.2.1.83) is an enzyme with systematic name 4-oxo-4-(pyridin-3-yl)butanal:NADP+ oxidoreductase. This enzyme catalyses the following chemical reaction
Pseudooxynicotine oxidase (EC 1.4.3.24) is an enzyme with systematic name 4-(methylamino)-1-(pyridin-3-yl)butan-1-one:oxygen oxidoreductase (methylamine releasing). This enzyme catalyses the following chemical reaction
2,4-dihydroxy-1,4-benzoxazin-3-one-glucoside dioxygenase (EC 1.14.20.2, BX6 (gene), DIBOA-Glc dioxygenase) is an enzyme with systematic name (2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside:oxygen oxidoreductase (7-hydroxylating). This enzyme catalyses the following chemical reaction
2,4-Dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-D-glucosyltransferase is an enzyme with systematic name UDP-alpha-D-glucose:2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one 2-beta-D-glucosyltransferase. This enzyme catalyses the following chemical reaction
4-Hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase (EC 3.2.1.182, DIMBOAGlc hydrolase, DIMBOA glucosidase) is an enzyme with systematic name (2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside beta-D-glucosidase. 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
Dichlorochromopyrrolate synthase (EC 1.21.3.9, RebD, dichlorochromopyrrolic acid synthase) is an enzyme with systematic name 2-imino-3-(7-chloroindol-3-yl)propanoate ammonia-lyase (dichlorochromopyrrolate-forming). This enzyme catalyses the following chemical reaction