`
`
`Reactive Surfaces Ltd. LLP
`Ex. 1019
`Reactive Surfaces Ltd. LLP v. Toyota Motor Corp.
`IPR2016-01914
`
`
`
`\
`'-
`
`ENZYME NOMENCLATURE
`
`1978
`
`RECOMMENDATIONS
`OF THE NOMENCLATURE
`COMMITTEE
`OF 1HE INTERNATIONAL
`UNION OF BIOCHEMISTRY
`ON THE
`NOMJ,lNCLATURE AND CLASSIFICATION
`OF EN2YMES
`
`This edition
`is a revision
`of the Recommendations
`(1972)
`of the IUPAC-IUB
`Commission
`on Biochemical
`Nomenclature,
`and has been approved for
`publication
`by the Executive
`Committee
`of the International
`Union of
`Biochemistry.
`
`
`..
`
`ACADEMIC
`PRESS New York San Francisco
`London 1979
`P11blis/1ed
`for Ille l,rfemntionnl
`U11io11
`of Biochemfst,y
`by Academic
`Press,
`Inc.
`
`9 Page 165
`
`
`
`Comment © 1979, or Amounts Puss, inc.
`ALL tumm- RESERVED.
`N0 nou- or Tam ronuunon may as REPRDDUCBD on
`mmmnao In my FORM on BY ANY mums, mac-memo
`on ”summon, mcwomo rHoToCon, “comma, on my
`tnromumon STORAGE AND RETRIEVAL svsmu. wrruom'
`PERMISSION m wm‘rmo mom THE puuusrrsn.
`
`ACADEMIC PRESS, INC.
`1:: FiithAvcnuu, New York. Now York [0001
`
`United Klufdom Edition publisher! by
`24(28 on! hold. London NW1
`ACADEM C PRESS. INC.71%0NDON) LTD.
`
`
`
`Revision of Enzyme nomenclature; recommendations ([972) of
`the Commission on Biochemical Nomenclature published in 1973.
`l. Enzymes—Nomenclature. 2. Enzymes—Classification. 1.
`II. Title.
`Commission on Biochemical Nomenclature. Enzyme nomenclature
`QPEOIJS-t 1919
`574.1'915'014
`19—1466
`
`Library a! Congxeas Cataloging In Publication Data
`
`International Union of Biochemistry. Nomenclature committee.
`Enzyme nomenclature. 1978.
`
`PRINTED 1N 'I‘IIE UNITED STATES OF AMERICA
`803152
`98765432
`
`9
`
`
`
`234
`
`Number
`
`
`
`Recommended Name
`
`Reaction
`
`name Is, In most cases, formed by the
`the reconimencled
`Includes 'hydrolasc',
`name always
`While the systematic
`with this sulf1X
`It is understood that the name of the substrate
`with the suffix -use.
`name of the substrate
`enzyme.
`means a hydrolytic
`
`3,1 ACTING ON ESTER BONDS
`thiolesterases
`(3. 1.2),
`(3.1.1),
`esters
`on cnrbo)(y!ic
`into those acting
`are subdivided
`The csterases
`hydrolases (3. 1.4),
`phosphodicster
`(3.IJ),
`the phosphatases
`triphosphoric monoester hydrolases (3.1.5), sulphatases (3.1.6),
`hydrolases,
`monoester
`phosphoric
`monoesterascs
`(3.1.7).
`and diphosphoric
`pla�d in a number of new sub-groups: the
`are now
`The nucleases, previously
`under 3.1.4,
`included
`(3.1.21-31).
`and lhe endonucleases
`ll-16)
`exonucleascs
`(3.1.
`
`
`
`3.1.1 CARBOXYLIC ESTER HYDR01ASES
`
`3.l.J.I Carboxyleste
`rase
`
`A carboxylic ester + H,O = an alcohol +
`
`
`a carboxylic acid anion
`
`3.J.l.2 Arylestcrase
`
`A phenyl acetate + H;O = a phenol +
`
`acetate
`
`
`
`3.1.l.3 Triacylglycerol lipase
`
`
`
`Triacylglycerol H10
`+
`fatly �cid anion
`
`diacylglycerol + a
`
`
`
`3.1.1.4 Phospholipase A1
`
`A lecithin + HiO =
`
`1-acylglycerophosphocholine + an
`
`
`
`unsaturated fatly acid anion
`
`3.1.1.5 Lysophospholipase
`
`A lysolecithin + H;O ""
`
`
`glycerophosphocholine a fatty acid anion
`+
`
`3.1.1.6 Acetylesterasc
`
`An acelic ester HiO � an alcohol
`
`
`+
`+
`acetate
`
`
`3.1.1.7 Acctylcholinesterase
`
`Acetylcholine + HiO -choline + acetate
`
`3.1.1.8 Cholinesterase
`
`a An acylcllpline + HiO = choline
`
`
`+
`
`carboxylic acid anion
`
`Ex. 1019 - Page 167
`
`
`
`Reference
`Comments
`Basis for classification
`Other Names
`
`' (Systemalic Name)
`
`235
`
`aloaml.+
`
`+
`
`+•
`
`133, 202, 288,
`Wide specificity. Also
`
`
`Carboxylic-ester hydrolase
`
`Ali-eslerase, B-eslerase,
`425, 1371, 2874
`
`hydrolyses vitamin A
`Mcthylbutyrase,
`esters
`
`Monobulyrase, Cocain
`
`estcrase, Procaine
`esterase
`
`47, 136, 2056,
`Acts on many phenolic
`Aryl-ester hydrolase
`
`A-esterase,
`347
`
`esters; the enzyme from
`Paraoxonase
`slieep serum also
`
`hydrolyses paraoxon
`
`1764, 2023,
`
`The pancreatic enzyme
`
`Triacylglyccrol acylhydrolase
`
`Steapsin,. Trihutyrase,
`2911, 3081
`acts only on an ester-
`
`Triglyceride lipase,
`
`water interface; the ouler
`Lipase
`ester links arc
`
`preferentially hydrolysed
`
`672, 736, 919,
`Also acts on
`Phosphatide 2-acylhydrolase
`
`Lecithinase A,
`
`1175, 2272, 2895
`phosphatidylethanolaminc,
`Phosphatidasc,
`
`
`choline plasmalogen and
`Phosphatidolipase
`
`phosphatides, removing
`
`the fatty acid attached to
`the 2-position
`
`anion
`
`
`Lysolecithin acylhydrolase
`3.J.1.5 Lccithinase B,
`
`Lysolecithinase,
`
`Phospholipase B
`
`574, 665, 855,
`3527
`
`+ acetate
`
`+ a
`
`3.1.1.6 C-esterasc (in animal
`
`
`tissues)
`
`Acetic.ester ncetylhydrolase
`
`47, 268, 1499
`
`3.1.1.7 Troe cholinesterase,
`
`Acetykholine ncetylhydrolase
`
`Acts on a variety of
`134, 269, 1928,
`
`
`Choline e.�tcrnse I,
`
`
`acetic esters; also
`2324, 3852, 540
`Cholinesterase
`
`catalyses transacetylations.
`
`..::l
`
`3.1.1.8 Pscudocholinesterase,
`
`Acylcholinc acylhydrolase
`Acts on a variety or
`
`134, 136, 1732,
`
`Butyrylcholine es!crasc,
`
`
`choline esters and a few
`2324, 2931, 3259
`
`
`Choline esterase II
`other compounds
`(unspecific),
`Benzoylcholinesterase
`
`Ltd., LLP Ex. 101 9 - Page 168Reactive Suriaces
`
`
`
`
`
`
`
`236
`
`Number
`
`
`
`Recommended Name
`
`Reaction
`
`{J.l.1.9
`
`
`
`
`
`a side reaction of EC 3.1.1.8} Deleted entry: Be11zoylcholi11esterose:
`
`3. l.1. 10 Tropincsterase
`
`+ HiO tropine + tropate
`Atropine
`
`3.1,1.11
`Pectinesterase
`
`Pectin + 11 H20 = n methanol + pectate
`
`
`
`[3.1.1.12 Deleted eniry:
`
`
`
`ev ed to be identical with EC 3.1.1.JJ now beliprevi<msly Vitami,1 A esterQse,
`
`
`
`
`
`
`
`3.1.1.13 Cholesterol esterase
`
`
`
`ester + H20 = cholesterol
`A chole�terol
`+
`a fatty acid anion
`
`
`
`3.1.1.14 Chlorophyllase
`
`+ H10 = phylol +
`Chlorophyll
`chlorophyllide
`
`
`
`3.1.1.15 Arahinonolactonase
`
`L·Arabinono-y-lactone
`+ H,O
`L-arabinonate
`
`{3.J.1./6 Deleted entry: This reacfio11
`
`
`
`
`
`
`3-oxoadipate-enol-lactone h.ydro/ase (EC 3.J.1.24)}
`
`
`
`was due to a mixllJre of mucono/actone isomerase (EC S.3.3.4) and
`
`3. I.I. l 7 Gluconolactonase
`
`
`
`T>-Glucono-8-lactone + HiO � o-gluconate
`
`3.1. I.18 Aldonolactonase
`
`
`
`L-Gulono-y•lactone + H,O gulonate
`
`
`
`3.1.l. I 9 Uronolactonase
`
`D-Glucurono·6-lactonc + H20=
`
`D-glucuronate
`
`3.1.1.20
`Tannase
`
`
`
`Digallate + HiO 2 gallate
`
`3.1.1.21
`
`
`Retinol-palmitate esterase
`
`Retinol palmitate + HiO = retinol
`
`
`+
`palmitale
`
`
`yryloxy)-butyrate + H10
`3. J.t.22 Hydrox yb1!lyra1
`
`rdimer hydrolase 3-u,{3-o-Hydroxybut
`= 2 J-o-hydroxybutyrate
`
`J.l.l.23
`
`
`Monoacylglycerol lipase
`
`Hydrolyses glycerol monoestcrs of long-chain
`
`
`
`
`falty acids
`
`
`3.1.1.24
`
`(l,4) + HiO
`3-0xoadipate · enol-lactonase
`4-Carboxymethylbut-3-enolide
`pate
`= 3-oxoadi
`
`3.1.1.25
`y-Lactonase
`
`
`
`y-Laclone + H;O - 4-hydroxyacid
`
`- - -- �
`--- -- -- -- --· - .. - . - - -- - �
`
`
`
`Reactive Surfaces Ltd., LLP Ex. 1019- Page 169
`
`
`
`Number Other Names
`
`237
`Basis for classification Comments Reference
`_Name)
`(Systematic
`
`3.1.1.10
`
`
`
`Also acts on cocaine and 1062, 2269
`
`Atropine acylhydtolase
`
`,,. other tropine esters
`
`. 3.l.1.11Pectin
`
`Pectin pectylhydrolase
`demethoxylase,
`
`Pectin metho1.ylase,
`
`methylesterase
`Pectin
`
`708, 1979, 2234
`
`3.1.1.13
`
`Also acts on esters of 442, 1290, 1781,
`
`Sterol·ester acylhydrolase
`
`some other sterols 3318
`
`3.1.1.14
`
`Chlorophyll Also catalyses 1343, 1712
`transfer, chlorophyllidoh ydrolase chlorophyllide
`
`
`
`e.g. converts chlorophyll
`lo methylchlorophyllide
`
`3.1.1.15
`
`L·Arabinono-y-lactone
`Jactonohydrolase
`
`3641
`
`
`
`3.1.1.17 Lactonnse
`
`D·Olucono-8-lactone
`lactonohydrolase
`
`L-Gulono-y-lactone
`lactonohydrolase
`
`3.1.1.18
`
`3.1.1.19
`
`3.1.1.20
`
`3.1.1.21
`
`3.1.1.22
`
`3.1.1.23
`
`3.1.1.24
`
`3.1.1.25
`
`391, 803
`
`415, 507
`
`o-Glucurono-8-laclone
`lactonohydrolase
`
`3706
`
`Tannin acylhydrolase Also hydrolyses ester 776
`
`links in other tannins
`
`Retinol-palmitate
`palmitohydrolase
`
`xybutyryloKy)·
`3-D-(3-1>-Hydro
`butyrate
`hydroxybutyrohydrolase
`
`2045
`
`688
`
`Glycerol-monoestcr
`acylhydrolase
`
`2636
`
`4-Carbollymethylbut-3-cnolide 1819
`(1,4) enol-laclonoliydrolase
`
`The enzyme is specific 887, 888
`y-Lactone
`for 4-8 carbon y-laclones.
`hydroxyacylhydrolase
`It does not hydrolyse
`
`
`simple aliphatic esters,
`
`Surfaces Ltd., LLP Ex. 101 9 - Page 170Reactive
`
`
`
`
`
`238
`Number
`
`Recommended
`Name
`
`Reaction
`
`,,
`
`3. 1.1.26 Galactolipase
`
`2,3-Di-0-acyl-I-O-(JJ-o-galactosyl)-D-glycerol
`+2 H,O = 1-0-(P-D-galactosyl)-D-glycerol
`+ 2 fatty acid anions
`
`3.1.1.27
`4-Pyridoxolaclonase
`4-Pyridoxolactone
`+ H,O 4-pyridoxate
`
`3. 1.1.28 Acylcarnitine
`hydrolase
`
`0-Acylcarnitine
`+ H,O a fatty acid +
`1.rcarnitine
`
`3.1. l .29 Aminoacyl-tRNA
`hydrolasc
`
`N-Substituted
`aminoacyl-tRNA
`+ H,O
`N-substituted
`amino acid + tRNA
`
`3. I. l .30 n-Arabinonolactonase
`D-Arabinono-y-lactone
`+ H,O -
`n-arabinonate
`
`3. 1 .1.31 6-Phosphogluconolactonase
`6-Phospho-n-gluconate
`8-lactone
`+ H10
`6-phospho-D-gluconate
`
`3.1. 1.32 Phospholipase
`A,
`
`A lecithin
`+ H,O �
`2-acylglycerophosphocholine
`+ a fatty acid
`anion
`
`3.1.1.33 6-0-Acetylglucose
`deacetylase
`glucose +
`6-0-Acetyl-n-glucose
`+ H,O
`acetate
`
`3.1.1.34
`Lipoprotein
`lipase
`
`Triacylglyccrol
`+ H,O = diacylglycerol
`+ a
`fatty acid anion
`
`3.1.1.35
`Dihydrocoumarin
`hydrolase
`
`Dihydrocoumarin
`+ HiO = melilotate
`
`3.1. 1.36 Limonin-D-ring-lactonase
`Limonoate
`D-ring-lactone
`+ H,O -
`Jimonoatc
`
`3.1.1.37 Steroid-lactonase
`
`Te.�tololnctone
`+ H,O = testolate
`
`Triacetate
`lactone + H,O = triacetate
`3. I. 1.38Triacetate-lactonase
`
`019 -Page 171
`Reactive Surfaces L
`td., LLP Ex. 1
`
`
`
`:lfumber Other Names
`
`Basis for classification Comments Reference
`
`(Systemalic Name)
`
`239
`
`}P-glycerol
`1)-o-glycerol
`
`3.1.1.26
`
`,.
`
`acetylcholine, sugar
`
`
`lactones or substituted
`
`aliphalic lactones,
`e.g.
`3-hydroxy-4-butyrolactone;
`
`requires Ca2 •
`
`1-0(/J-l>-
`2,3-Di-O-acyl-
`Also acts on 2,3-di-0-1270, 1321
`galactosyl)-o-glycerol
`acyl-1-0-(6-0-<1-P-
`acylhydrolase galactosyl-/1-D-galactosyl)-
`
`o-glycerol, and
`
`phosphalidylcholine and
`other phospholipids
`
`4-pyridoxate
`
`3.1.1.27
`
`4-Pyridoxolactone
`lactonohydrolase
`
`427
`
`fatly acid +
`
`3.1.1.28
`
`3.1.1.29
`
`3.1.1.30
`
`3.1.1.31
`
`0-Acylcarnitine acylhydrolasc
`
`
`Acls on higher fatly acid 2046
`
`(C-6 lo C-18) esters of L·
`
`carnitine; highest activity
`is with
`0-decanoyl-L-camitine
`
`Aminoacyl-lRNA
`anunoacylhydrolase
`
`1538
`
`o-Arabinono-y-Jactone
`lactonohydrolase
`
`2546
`
`6-Phospho-p-gluconate-6-Jactone
`1624
`laclonohydrolase
`
`a fatty acid
`
`3.1.1.32
`
`
`
`Phosphatidate 1-acylhydrolase
`
`997
`
`
`
`glucose +
`
`3.1.1.33
`
`6-0-Acctyl-o-glucose
`acetylhydrolase
`
`765
`
`3.J.1.34
`�,
`
`Clearing factor lipas,
`Triacylglycero-protein
`
`Hydrolyses triacylglycerols
`878, Ill 8, 796,
`
`Diglyceride lipase,
`
`acylhydrolase in chylomicrons and low•
`2293, 2411
`
`Diacylglycerol lipase
`
`
`densily lipoproteins. Also
`
`hydrolyses diacylglycerol
`
`3.1.1.35
`
`3.1.1.36
`
`Dihydrocoumarin Also hydrolyses some 1784
`
`lactonohydrolase
`
`other benzenoid y-lactones
`
`Limonqate-D-ring-lactone 2055
`lactonohydrolase
`
`3.1.1.37
`
`
`
`Testololactone lactonohydrolase
`
`late
`
`3.1. 1.38
`
`Triacetolactonc
`Jactonohydrolasc
`
`1351
`
`1608
`
`Ltd., LLP Ex. 1019- Page 172
`Reactive Surfaces
`
`