mercapto protease

mercapto protease (plural mercapto proteases)

2005, "Proceedings on Rose Breeding, Cultivation and Production in China", Y Lin, Q Liu, IV International Symposium on Rose Research and Cultivation, actahort.org
Mercapto-protease and serine protease were both found in rose petals.

The protease may be mercapto protease, preferably papain.

2017, December 8, Chenguang Biotech Group Co Ltd, "Lycopene micro-capsule powder and preparation method therefor", European Patent Office EP3721874A1

2020, "Electrochemical detection of silver ions by using sulfur quantum dots modified gold electrode", L Fu, A Wang, K Xie, J Zhu, F Chen, H Wang, et al., Sensors and Actuators B: Chemical, Elsevier
The principle is that silver ion can inhibit the activity of free mercapto protease and thus inhibit its biological function [[4], [5], [6]].

Considering that papain is a mercapto protease enzyme, and sulfydryl groups of papain are deemed to show a strong affinity for Au and Ag (as was the case for BSA).

2020, X LiuY ZhangS WangC LiuT WangZ Qiuet al., “Performance comparison of surface plasmon resonance biosensors based on ultrasmall noble metal nanoparticles templated using bovine serum albumin”, in Microchemical Journal, Elsevier:

2021, "Cloning, expression and characterization of metalloproteinase HypZn from Aspergillus niger", P Song, W Xu, K Wang, Y Zhang, F Wang, X Zhou, et al., PLoS one, journals.plos.org
The cysteine protease inhibitor E-64 had little effect on enzyme activity, indicating that the HypZn active site does not contain cysteine and that it is not a mercaptoprotease.

(biochemistry) A protease that contains an active sulfhydryl group.


electroenzyme

(biochemistry) Any enzyme that catalyses an electrochemical reaction


kexin

en-noun

kexin (countable and uncountable, plural kexins)

(biochemistry) A yeast serine peptidase.


cerliponase

(biochemistry) A peptidase that acts on tripeptides


melanoproteinase

(biochemistry) Any proteinase that acts on a melanoprotein


sarcinopterin

(biochemistry) A derivative of methanopterin


miniproteinase

(biochemistry) A relatively small proteinase


citrullinase

(biochemistry) Any enzyme that hydrolyses citrulline to produce ornithine


salikase

(biochemistry) An enzyme capable of hydrolyzing salicin to dextrose and saligenin.


ammonialyase

(biochemistry) Any enzyme that converts an amine into ammonia


phosphofructomutase

(biochemistry) Any enzyme that catalyzes the interconversion of isomers of fructose phosphates


photokinase

(biochemistry) A kinase involved with photokinesis


phosphonatase

(biochemistry) Any enzyme that hydrolyses phosphonates


sarcosinase

(biochemistry) An enzyme that hydrolyses sarcosine moieties from proteins


phosphoglycosyltransferase

(biochemistry) Any enzyme that catalyses the transfer of a phosphoglycosyl group


biotransferase

(biochemistry) Any naturally-occurring transferase


PEMT

PEMT (countable and uncountable, plural PEMTs)

(biochemistry) Initialism of phosphatidylethanolamine N-methyltransferase.


glucosamidase

(biochemistry) An enzyme that hydrolyses glucosamide


CAPP

(biochemistry) Acronym of ceramide-activated protein phosphatase.


L-xylulokinase

L-xylulokinase (countable and uncountable, plural L-xylulokinases)

adenosine triphosphate
adenosine triphosphate

adenosine diphosphate
adenosine diphosphate

L-xylulose 5-phosphate
L-xylulose 5-phosphate

(biochemistry) An enzyme that catalyzes ATP (adenosine triphosphate) and L-xylulose, producing ADP (adenosine diphosphate) and L-xylulose 5-phosphate. It's a phosphotransferase used in metabolism.


Elapid venoms mainly comprise peptides and proteins from seven families; secreted phospholipases A2 (PLA2s)^(32,33,34,35,36) and three-finger toxins (3FTxs)^(36,37,38,39) are often major constituents and have a dominant role in the action of the venom, […]

2022 June 10, Oliveira, A.L., Viegas, M.F., da Silva, S.L. et al., “The chemistry of snake venom and its medicinal potential”, in Nature Reviews Chemistry, volume 6, →DOI, page 453:

(biochemistry) Abbreviation of phospholipase A2.


SVSP

Other toxins — namely snake venom metalloproteinases (SVMPs)^(34,36,40,41,42), snake venom serine proteases (SVSPs)^(34,36,43) and l-amino acid oxidases (LAAOs)^(34,44,45,46,47) — represent an average of 6% of elapid venom.

(biochemistry) Initialism of snake venom serine protease.


LAAO

L-amino-acid oxidase
w:L-amino-acid oxidase

(biochemistry) Initialism of L-amino-acid oxidase.


SVMP

(biochemistry) Initialism of snake venom metalloproteinase.


BuChE

Coordinate term: AChE

(biochemistry) Abbreviation of butyrylcholinesterase.


AChE

Coordinate term: BuChE

(biochemistry) Abbreviation of acetylcholinesterase.


glucose-6-phosphate isomerase

glucose-6-phosphate isomerase (plural glucose-6-phosphate isomerases)

fructose 6-phosphate
fructose 6-phosphate

(biochemistry) An enzyme that catalyzes intercellular the interconversion of glucose 6-phosphate (G6P) and fructose 6-phosphate (F6P) and functions extracellular as a neurotrophic factor and lymphokine.


AMPK

AMP-activated protein kinase
w:AMP-activated protein kinase

(biochemistry) Initialism of AMP-activated protein kinase.

(acetyl-CoA carboxylase) kinase
w:(acetyl-CoA carboxylase) kinase

(biochemistry) Initialism of (acetyl-CoA carboxylase) kinase.


alcohol dehydrogenase

alcohol dehydrogenase (plural alcohol dehydrogenases)

(biochemistry) An enzyme that catalyzes the oxidation of alcohols to aldehydes or ketones.


JAK

(biochemistry) Initialism of Janus kinase.


butyrinase

(biochemistry) The enzyme triacylglycerol lipase, which catalyzes the hydrolysis of ester linkages of triglycerides.


phosphatidyltransferase

phosphatidyltransferase (countable and uncountable, plural phosphatidyltransferases)

Steps that follow the formation of archaeal phospholipids are the activation of CDP-archaeol by CarS […] and head group modification by enzymes of the CPD-alcohol phosphatidyltransferases and by enzymes that are homologues of their bacterial counterparts.

2016, Pierre Pontarotti, Evolutionary Biology: Convergent Evolution, Evolution of Complex Traits, Concepts and Methods, page 196:

(biochemistry) An enzyme that catalyzes the transfer of a phosphatidyl group from one molecule to another, involved in lipid metabolism and cell membrane synthesis.