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Literature summary for 3.2.1.147 extracted from

  • Nakano, R.T.; Pislewska-Bednarek, M.; Yamada, K.; Edger, P.P.; Miyahara, M.; Kondo, M.; Boettcher, C.; Mori, M.; Nishimura, M.; Schulze-Lefert, P.; Hara-Nishimura, I.; Bednarek, P.
    PYK10 myrosinase reveals a functional coordination between endoplasmic reticulum bodies and glucosinolates in Arabidopsis thaliana (2017), Plant J., 89, 204-220 .
    View publication on PubMed
Search for more literature for 3.2.1.147

Cloned(Commentary)

Cloned (Comment) Organism
phylogenetic analysis and tree, recombinant expression of wild-type and mutant enzymes Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
E418A site-directed mutagenesis, inactive catalytic site mutant Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining
endoplasmic reticulum body endoplasmic reticulum (ER) bodies in Arabidopsis thaliana contain large amounts of beta-glucosidases, and PYK10 is the most abundant beta-glucosidase in root ER bodies Arabidopsis thaliana
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Arabidopsis thaliana indole glucosinolates are in planta substrates for PYK10 ?
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 ?

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
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Source Tissue

Source Tissue Comment Organism Textmining
root
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 Arabidopsis thaliana
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4-methylumbelliferyl-beta-D-glucoside + H2O
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 Arabidopsis thaliana 4-methylumbelliferone + D-glucose
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 ?
indol-3-ylmethyl glucosinolate + H2O high activity Arabidopsis thaliana indo-3-ylmethyl isothiocyanate + D-glucose
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 ?
additional information indole glucosinolates are in planta substrates for PYK10 Arabidopsis thaliana ?
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 ?
additional information enzyme PYK10 has in vitro myrosinase activity toward indole glucosinolates. PYK10 exhibits both O-glucosidase and S-glucosidase activity. No activity against sinigrin. PYK10 hydrolyzes both coumarin glucosides and glucosinolates, and accounts for the bulk of total myrosinase activity against indol-3-ylmethyl glucosinolate in Arabidopsis thaliana roots Arabidopsis thaliana ?
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 ?
scopolin + H2O
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 Arabidopsis thaliana ?
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 ?

Synonyms

Synonyms Comment Organism
PYK10 myrosinase
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 Arabidopsis thaliana

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
5.5
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 narrow optimum Arabidopsis thaliana

General Information

General Information Comment Organism
evolution in silico three-dimensional modeling, combined with phylogenomic analysis, suggests that PYK10 represents a clade of 16 myrosinases that arose independently from the other well-documented class of six thioglucoside glucohydrolases. Phylogenomic and three-dimensional structural modeling analysis identified the presence of two independent classes of myrosinases, represented by PYK10/PEN2 and thioglucoside glucohydrolases (TGGs). Analysis of evolutionary origin of myrosinases, overview. Gene modules composed of IG modification, hydrolysis and catabolism genes may facilitate a functional differentiation among myrosinases Arabidopsis thaliana
physiological function PYK10, the most abundant beta-glucosidase in Arabidopsis thaliana root endoplasmic reticulum (ER) bodies, hydrolyzes indole glucosinolates (IGs) in addition to the previously reported in vitro substrate scopolin. PYK10 myrosinase reveals a functional coordination between endoplasmic reticulum bodies and glucosinolates in Arabidopsis thaliana. Variation of the myrosinase-glucosinolate system exists within individual plants. The co-expressed gene cluster of PYK10 is enriched in genes required for the production of glucosinolates. Glucosinolates are in planta substrates for PYK10 that are tightly linked to the physiological functions of ER bodies. ER bodies are potentially engaged in plant-microbe interactions via indole glucosinolate metabolism and in abiotic stress responses via coumarin metabolism Arabidopsis thaliana