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(S)-hydroxynitrile lyase (EC 4.1.2.47) ((S)-acetone-cyanohydrin lyase) (Oxynitrilase)

 HNL_HEVBR               Reviewed;         257 AA.
P52704;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
15-FEB-2017, entry version 86.
RecName: Full=(S)-hydroxynitrile lyase;
EC=4.1.2.47;
AltName: Full=(S)-acetone-cyanohydrin lyase;
AltName: Full=Oxynitrilase;
Name=HNL;
Hevea brasiliensis (Para rubber tree) (Siphonia brasiliensis).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; rosids; fabids; Malpighiales; Euphorbiaceae;
Crotonoideae; Micrandreae; Hevea.
NCBI_TaxID=3981;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 121-126; 176-181;
200-204 AND 244-253, AND MUTAGENESIS OF CYS-81.
TISSUE=Leaf;
PubMed=8621461; DOI=10.1074/jbc.271.10.5884;
Hasslacher M., Schall M., Hayn M., Griengl H., Kohlwein S.D.,
Schwab H.;
"Molecular cloning of the full-length cDNA of (S)-hydroxynitrile lyase
from Hevea brasiliensis. Functional expression in Escherichia coli and
Saccharomyces cerevisiae and identification of an active site
residue.";
J. Biol. Chem. 271:5884-5891(1996).
[2]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND MUTAGENESIS OF SER-80 AND
HIS-235.
PubMed=8805565; DOI=10.1016/S0969-2126(96)00088-3;
Wagner U.G., Hasslacher M., Griengl H., Schwab H., Kratky C.;
"Mechanism of cyanogenesis: the crystal structure of hydroxynitrile
lyase from Hevea brasiliensis.";
Structure 4:811-822(1996).
[3]
X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS).
PubMed=10494852; DOI=10.1515/BC.1999.123;
Gruber K., Gugganig M., Wagner U.G., Kratky C.;
"Atomic resolution crystal structure of hydroxynitrile lyase from
Hevea brasiliensis.";
Biol. Chem. 380:993-1000(1999).
[4]
X-RAY CRYSTALLOGRAPHY (1.72 ANGSTROMS).
PubMed=10548044; DOI=10.1110/ps.8.10.1990;
Zuegg J., Gruber K., Gugganig M., Wagner U.G., Kratky C.;
"Three-dimensional structures of enzyme-substrate complexes of the
hydroxynitrile lyase from Hevea brasiliensis.";
Protein Sci. 8:1990-2000(1999).
-!- FUNCTION: Involved in cyanogenesis, the release of HCN from
injured tissues. Decomposes a varieties of (R) or (S) cyanohydrins
into HCN and the corresponding aldehydes and ketones. The natural
substrate of this enzyme is (S)-acetone cyanohydrin.
-!- CATALYTIC ACTIVITY: An aliphatic (S)-hydroxynitrile = cyanide + an
aliphatic aldehyde or ketone.
-!- CATALYTIC ACTIVITY: An aromatic (S)-hydroxynitrile = cyanide + an
aromatic aldehyde.
-!- SUBUNIT: Homodimer.
-!- PTM: The N-terminus is blocked.
-!- SIMILARITY: Belongs to the AB hydrolase superfamily.
Hydroxynitrile lyase family. {ECO:0000305}.
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EMBL; U40402; AAC49184.1; -; mRNA.
PIR; T10758; T10758.
PDB; 1QJ4; X-ray; 1.10 A; A=1-257.
PDB; 1SC9; X-ray; 1.80 A; A=1-257.
PDB; 1SCI; X-ray; 2.18 A; A=1-257.
PDB; 1SCK; X-ray; 1.70 A; A=1-257.
PDB; 1SCQ; X-ray; 2.90 A; A=1-257.
PDB; 1YAS; X-ray; 1.90 A; A=1-257.
PDB; 1YB6; X-ray; 1.54 A; A=2-257.
PDB; 1YB7; X-ray; 1.76 A; A=2-257.
PDB; 2G4L; X-ray; 1.84 A; A=1-257.
PDB; 2YAS; X-ray; 1.72 A; A=1-257.
PDB; 3C6X; X-ray; 1.05 A; A=1-257.
PDB; 3C6Y; X-ray; 1.25 A; A=1-257.
PDB; 3C6Z; X-ray; 1.05 A; A=1-257.
PDB; 3C70; X-ray; 1.05 A; A=1-257.
PDB; 3YAS; X-ray; 1.85 A; A=1-257.
PDB; 4YAS; X-ray; 2.00 A; A=1-257.
PDB; 5YAS; X-ray; 2.20 A; A=1-257.
PDB; 6YAS; X-ray; 2.20 A; A=1-257.
PDB; 7YAS; X-ray; 1.75 A; A=1-257.
PDBsum; 1QJ4; -.
PDBsum; 1SC9; -.
PDBsum; 1SCI; -.
PDBsum; 1SCK; -.
PDBsum; 1SCQ; -.
PDBsum; 1YAS; -.
PDBsum; 1YB6; -.
PDBsum; 1YB7; -.
PDBsum; 2G4L; -.
PDBsum; 2YAS; -.
PDBsum; 3C6X; -.
PDBsum; 3C6Y; -.
PDBsum; 3C6Z; -.
PDBsum; 3C70; -.
PDBsum; 3YAS; -.
PDBsum; 4YAS; -.
PDBsum; 5YAS; -.
PDBsum; 6YAS; -.
PDBsum; 7YAS; -.
ProteinModelPortal; P52704; -.
SMR; P52704; -.
ESTHER; hevbr-hnl; Hydroxynitrile_lyase.
PRIDE; P52704; -.
KEGG; ag:AAC49184; -.
KO; K13033; -.
BRENDA; 4.1.2.47; 2665.
EvolutionaryTrace; P52704; -.
GO; GO:0052891; F:aliphatic (S)-hydroxynitrile lyase activity; IEA:UniProtKB-EC.
GO; GO:0052892; F:aromatic (S)-hydroxynitrile lyase activity; IEA:UniProtKB-EC.
Gene3D; 3.40.50.1820; -; 1.
InterPro; IPR029058; AB_hydrolase.
InterPro; IPR000073; AB_hydrolase_1.
Pfam; PF00561; Abhydrolase_1; 1.
SUPFAM; SSF53474; SSF53474; 1.
1: Evidence at protein level;
3D-structure; Direct protein sequencing; Lyase.
CHAIN 1 257 (S)-hydroxynitrile lyase.
/FTId=PRO_0000084017.
DOMAIN 5 241 AB hydrolase-1. {ECO:0000255}.
ACT_SITE 80 80
ACT_SITE 207 207
ACT_SITE 235 235
MUTAGEN 80 80 S->A: Loss of activity.
{ECO:0000269|PubMed:8805565}.
MUTAGEN 81 81 C->S: Loss of activity.
{ECO:0000269|PubMed:8621461}.
MUTAGEN 235 235 H->A: Loss of activity.
{ECO:0000269|PubMed:8805565}.
STRAND 5 9 {ECO:0000244|PDB:3C6X}.
HELIX 16 19 {ECO:0000244|PDB:3C6X}.
HELIX 22 28 {ECO:0000244|PDB:3C6X}.
STRAND 32 36 {ECO:0000244|PDB:3C6X}.
HELIX 48 50 {ECO:0000244|PDB:3C6X}.
HELIX 54 57 {ECO:0000244|PDB:3C6X}.
HELIX 59 66 {ECO:0000244|PDB:3C6X}.
STRAND 74 80 {ECO:0000244|PDB:3C6X}.
HELIX 82 93 {ECO:0000244|PDB:3C6X}.
HELIX 94 96 {ECO:0000244|PDB:3C6X}.
STRAND 97 105 {ECO:0000244|PDB:3C6X}.
STRAND 110 112 {ECO:0000244|PDB:3C6X}.
HELIX 116 124 {ECO:0000244|PDB:3C6X}.
STRAND 132 138 {ECO:0000244|PDB:3C6X}.
STRAND 141 147 {ECO:0000244|PDB:3C6X}.
HELIX 150 156 {ECO:0000244|PDB:3C6X}.
HELIX 163 172 {ECO:0000244|PDB:3C6X}.
HELIX 180 185 {ECO:0000244|PDB:3C6X}.
TURN 191 193 {ECO:0000244|PDB:3C6X}.
HELIX 194 196 {ECO:0000244|PDB:3C6X}.
STRAND 199 203 {ECO:0000244|PDB:3C6X}.
STRAND 208 210 {ECO:0000244|PDB:3C6X}.
HELIX 212 221 {ECO:0000244|PDB:3C6X}.
STRAND 225 229 {ECO:0000244|PDB:3C6X}.
HELIX 237 240 {ECO:0000244|PDB:3C6X}.
HELIX 242 255 {ECO:0000244|PDB:3C6X}.
SEQUENCE 257 AA; 29228 MW; EF4AE88717279CEB CRC64;
MAFAHFVLIH TICHGAWIWH KLKPLLEALG HKVTALDLAA SGVDPRQIEE IGSFDEYSEP
LLTFLEALPP GEKVILVGES CGGLNIAIAA DKYCEKIAAA VFHNSVLPDT EHCPSYVVDK
LMEVFPDWKD TTYFTYTKDG KEITGLKLGF TLLRENLYTL CGPEEYELAK MLTRKGSLFQ
NILAKRPFFT KEGYGSIKKI YVWTDQDEIF LPEFQLWQIE NYKPDKVYKV EGGDHKLQLT
KTKEIAEILQ EVADTYN


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