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Aliphatic (R)-hydroxynitrile lyase (LuHNL) (EC 4.1.2.46)

 AHNL_LINUS              Reviewed;         422 AA.
P93243; O22574;
25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
01-MAY-1997, sequence version 1.
23-MAY-2018, entry version 78.
RecName: Full=Aliphatic (R)-hydroxynitrile lyase;
Short=LuHNL;
EC=4.1.2.46;
Linum usitatissimum (Flax) (Linum humile).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Malpighiales; Linaceae; Linum.
NCBI_TaxID=4006;
[1]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=9030531; DOI=10.1074/jbc.272.8.4770;
Trummler K., Wajant H.;
"Molecular cloning of acetone cyanohydrin lyase from flax (Linum
usitatissimum). Definition of a novel class of hydroxynitrile
lyases.";
J. Biol. Chem. 272:4770-4774(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 15-47.
Breithaupt H., Pohl M., Boenigk W., Heim P., Schimz K.-L., Kula M.-R.;
"Cloning and expression of (R)-hydroxynitrile lyase from Linum
usitatissimum (flax).";
J. Mol. Catal., B Enzym. 6:315-332(1999).
[3]
PROTEIN SEQUENCE OF 9-47, AND CATALYTIC ACTIVITY.
PubMed=8387315;
Albrecht J., Jansen I., Kula M.R.;
"Improved purification of an (R)-oxynitrilase from Linum usitatissimum
(flax) and investigation of the substrate range.";
Biotechnol. Appl. Biochem. 17:191-203(1993).
[4]
CHARACTERIZATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
PubMed=3377504; DOI=10.1016/0003-9861(88)90634-0;
Xu L.L., Singh B.K., Conn E.E.;
"Purification and characterization of acetone cyanohydrin lyase from
Linum usitatissimum.";
Arch. Biochem. Biophys. 263:256-263(1988).
[5]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF CYS-63;
THR-65; GLY-84; HIS-85; GLY-95; GLY-104; CYS-118; CYS-129 AND CYS-199.
DOI=10.1016/S0168-9452(98)00173-3;
Trummler K., Roos J., Schwaneberg U., Effenberger F., Foerster S.,
Pfizenmaier K., Wajant H.;
"Expression of the Zn(2+)-containing hydroxynitrile lyase from flax
(Linum usitatissimum) in Pichia pastoris - utilization of the
recombinant enzyme for enzymatic analysis and site-directed
mutagenesis.";
Plant Sci. 139:19-27(1998).
-!- FUNCTION: Involved in the catabolism of cyanogenic glycosides.
Naturally occurring substrates are the aliphatic acetone
cyanohydrin and butan-2-one cyanohydrin, which are the aglycones
of the cyanogenic glycosides linamarin, lotaustralin, linustatin
and neolinustatin. Can use various aliphatic ketones and aldehydes
as substrates, but not aromatic ketones. {ECO:0000269|Ref.5}.
-!- CATALYTIC ACTIVITY: (2R)-2-hydroxy-2-methylbutanenitrile = cyanide
+ butan-2-one. {ECO:0000269|PubMed:8387315, ECO:0000269|Ref.5}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|Ref.5};
Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|Ref.5};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=1.9 mM for acetone cyanohydrin {ECO:0000269|PubMed:3377504,
ECO:0000269|PubMed:9030531};
Vmax=71 umol/min/mg enzyme with acetone cyanohydrin as substrate
{ECO:0000269|PubMed:3377504, ECO:0000269|PubMed:9030531};
pH dependence:
Optimum pH is 5.5. {ECO:0000269|PubMed:3377504,
ECO:0000269|PubMed:9030531};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:3377504}.
-!- MISCELLANEOUS: In contrast to the enzyme from rosaceae, this
enzyme is not glycosylated and does not contain FAD. Not inhibited
by reagents interfering with Zn(2+) coordination.
-!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
family. {ECO:0000305}.
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EMBL; Y09084; CAA70304.1; -; mRNA.
EMBL; AF024588; AAB81956.1; -; mRNA.
PIR; T07967; T07967.
ProteinModelPortal; P93243; -.
SMR; P93243; -.
PRIDE; P93243; -.
KEGG; ag:CAA70304; -.
KO; K14577; -.
BioCyc; MetaCyc:MONOMER-15903; -.
BRENDA; 4.1.2.46; 3037.
GO; GO:0052920; F:(2R)-2-hydroxy-2-methylbutanenitrile lyase activity; IEA:UniProtKB-EC.
GO; GO:0052921; F:acetone-cyanohydrin acetone-lyase (cyanide-forming) activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro.
InterPro; IPR013149; ADH_C.
InterPro; IPR013154; ADH_N.
InterPro; IPR011032; GroES-like_sf.
InterPro; IPR036291; NAD(P)-bd_dom_sf.
Pfam; PF08240; ADH_N; 1.
Pfam; PF00107; ADH_zinc_N; 1.
SUPFAM; SSF50129; SSF50129; 1.
SUPFAM; SSF51735; SSF51735; 1.
1: Evidence at protein level;
Direct protein sequencing; Lyase; Metal-binding; Zinc.
CHAIN 1 422 Aliphatic (R)-hydroxynitrile lyase.
/FTId=PRO_0000415393.
METAL 63 63 Zinc 1; catalytic. {ECO:0000250}.
METAL 85 85 Zinc 1; catalytic. {ECO:0000250}.
METAL 115 115 Zinc 2. {ECO:0000250}.
METAL 118 118 Zinc 2. {ECO:0000250}.
METAL 121 121 Zinc 2. {ECO:0000250}.
METAL 129 129 Zinc 2. {ECO:0000250}.
METAL 199 199 Zinc 1; catalytic. {ECO:0000250}.
MUTAGEN 63 63 C->A: Loss of activity.
{ECO:0000269|Ref.5}.
MUTAGEN 65 65 T->A: Loss of activity.
{ECO:0000269|Ref.5}.
MUTAGEN 84 84 G->A: Loss of activity.
{ECO:0000269|Ref.5}.
MUTAGEN 85 85 H->A: Loss of activity.
{ECO:0000269|Ref.5}.
MUTAGEN 95 95 G->A: Loss of activity.
{ECO:0000269|Ref.5}.
MUTAGEN 104 104 G->A: 90% reduction of activity.
{ECO:0000269|Ref.5}.
MUTAGEN 118 118 C->A: Loss of activity.
{ECO:0000269|Ref.5}.
MUTAGEN 129 129 C->A: Loss of activity.
{ECO:0000269|Ref.5}.
MUTAGEN 199 199 C->A: Loss of activity.
{ECO:0000269|Ref.5}.
CONFLICT 117 117 V -> T (in Ref. 2; AAB81956).
{ECO:0000305}.
SEQUENCE 422 AA; 45783 MW; 178901103F1783FF CRC64;
MASLPVSFAK PDKNGVITCK AIMLKEAKLP GMSYADTVQI IDIQVDPPQN VELRVKMLCA
SVCRTDILTI EGFMAPTQFP KINGHEGVGI IESMGPDTKN FKVGDVIVAP TLGECQVCSS
CRSGRTNFCQ NYGANESALE PDGTSRFSYI DSDGKKKLLY YKLGCSTWTQ YMVVDSNYAT
KLNEIAPELP PPHGSILSCA FATGYGAVWL DAAVQEGDSV AIFGVGSVGI SAVIAAKELK
AKQIIVVDRN EYKLKMAMEL GATHCINSEK LPEGVTPSQA VRKLTPKEVG VDASIESSGY
DVFMNEAMKA AIHGKAKTVI TGEGIYENDR IFFDFKDFLF GGNVVGNVTG RVRIHSDFPG
LLRKAQEPVI RAGMDKILGY DAATMKCKYE VDIREGTPAL LKALEEVENV DCVKLVIKLN
DY


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