KEGG   ENZYME: 4.8.1.5
Entry
EC 4.8.1.5                  Enzyme                                 
Name
thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming);
NSP (gene name);
nitrile-specifier protein
Class
Lyases;
Nitrogen-oxygen lyases;
Hydro-lyases
Sysname
thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming)
Reaction(IUBMB)
an N-(sulfonatooxy)alkanimidothioate = a nitrile + sulfate + sulfur [RN:R13121]
Reaction(KEGG)
R13121
Substrate
N-(sulfonatooxy)alkanimidothioate [CPD:C22630]
Product
nitrile [CPD:C00726];
sulfate [CPD:C00059];
sulfur [CPD:C00087]
Comment
The enzyme is involved in the breakdown of glucosinolates. It can act on both aliphatic and aromatic glucosinolates, and forms nitrile-containing products. cf. EC 4.8.1.6, N-(sulfonatooxy)alkenimidothioic acid sulfate-lyase (epithionitrile-forming), and EC 4.8.1.7, phenyl-N-(sulfonatooxy)methanimidothioate sulfolyase.
History
EC 4.8.1.5 created 2022
Orthology
K26380  thiohydroximate-O-sulfate sulfate/sulfur-lyase (nitrile-forming)
Genes
ATH: AT2G33070(NSP2) AT3G16390(NSP3) AT3G16400(NSP1) AT3G16410(NSP4) AT5G48180(NSP5)
ALY: 9298633 9301691 9315498 9321205 9321206
CRB: 17875885 17891128 17893216
CSAT: 104725304 104745971 104745975 104765478 104765479 104765481 104770869 104781292
EUS: EUTSA_v10004595mg EUTSA_v10020667mg
BRP: 103840057 103847838 103854522 103869760 103869761 103874933
BNA: 106348971 106381025 106428949 106428974 106452130 106452131 106454060 111198713 111203366 125603759
BOE: 106292512 106295641 106295642 106301248 106316308 106326669
RSZ: 108812649 108825069 108838726 108848670 108861513 130495939
THJ: 104802626 104822434
Reference
1  [PMID:19224919]
  Authors
Kissen R, Bones AM.
  Title
Nitrile-specifier proteins involved in glucosinolate hydrolysis in Arabidopsis thaliana.
  Journal
J Biol Chem 284:12057-70 (2009)
DOI:10.1074/jbc.M807500200
  Sequence
[ath:AT2G33070]
Reference
2  [PMID:18987211]
  Authors
Burow M, Losansky A, Muller R, Plock A, Kliebenstein DJ, Wittstock U.
  Title
The genetic basis of constitutive and herbivore-induced ESP-independent nitrile formation in Arabidopsis.
  Journal
Plant Physiol 149:561-74 (2009)
DOI:10.1104/pp.108.130732
  Sequence
[ath:AT3G16400 AT2G33070 AT3G16390 AT3G16410 AT5G48180]
Other DBs
ExplorEnz - The Enzyme Database: 4.8.1.5
IUBMB Enzyme Nomenclature: 4.8.1.5
ExPASy - ENZYME nomenclature database: 4.8.1.5
BRENDA, the Enzyme Database: 4.8.1.5
LinkDB

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