KEGG ENZYME: 1.14.99.53

ENZYME: 1.14.99.53

Entry

EC 1.14.99.53               Enzyme

Name

lytic chitin monooxygenase;
LPMO (ambiguous);
CBP21;
chitin oxidohydrolase

Class

Oxidoreductases;
Acting on paired donors, with incorporation or reduction of molecular oxygen;
Miscellaneous

Sysname

chitin, hydrogen-donor:oxygen oxidoreductase (N-acetyl-beta-D-glucosaminyl C1-hydroxylating/C4-dehdyrogenating)

Reaction(IUBMB)

[(1->4)-N-acetyl-beta-D-glucosaminyl](m+n) + reduced acceptor + O2 = [(1->4)-N-acetyl-beta-D-glucosaminyl](m-1)-(1->4)-2-(acetylamino)-2-deoxy-D-glucono-1,5-lactone + [(1->4)-N-acetyl-beta-D-glucosaminyl]n + acceptor + H2O [RN:R11660]

Reaction(KEGG)

R11660

Substrate

[(1->4)-N-acetyl-beta-D-glucosaminyl](m+n);
reduced acceptor [CPD:C00030];
O2 [CPD:C00007]

Product

[(1->4)-N-acetyl-beta-D-glucosaminyl](m-1)-(1->4)-2-(acetylamino)-2-deoxy-D-glucono-1,5-lactone;
[(1->4)-N-acetyl-beta-D-glucosaminyl]n;
acceptor [CPD:C00028];
H2O [CPD:C00001]

Comment

The enzyme cleaves chitin in an oxidative manner, releasing fragments of chitin with an N-acetylamino-D-glucono-1,5-lactone at the reducing end. The initially formed lactone at the reducing end of the shortened chitin chain quickly hydrolyses spontaneously to the aldonic acid. In vitro ascorbate can serve as reducing agent. The enzyme contains copper at the active site.

History

EC 1.14.99.53 created 2017

Orthology

K21713

lytic chitin monoxygenase

Genes

BAN:

BA_2827

BAR:

GBAA_2827

BAT:

BAS2636

BAH:	BAMEG_1769

BAI:

BAA_2889

BAX:	H9401_2696

BANT:

A16_28600

BANR:

A16R_29030

BANS:

BAPAT_2716

BANH:

HYU01_14015

BANV:

DJ46_1602(cbp)

BCE:

BC2827

BCA:

BCE_2855

BCZ:	BCE33L2552(chb)

BCR:	BCAH187_A2876

BCB:	BCB4264_A2838

BCU:	BCAH820_2833

BCG:	BCG9842_B2455

BCQ:	BCQ_2665(chb)

BCX:

BCA_2908

BAL:	BACI_c27900(chb2)

BNC:

BCN_2687

BCF:

bcf_13835

BCER:

BCK_20740

BCEF:

BcrFT9_02220

BCY:	Bcer98_1926

BTK:	BT9727_2586(chb)

BTL:

BALH_2536

BTB:	BMB171_C2529

BTT:

HD73_3152

BTHR:

YBT1520_15540

BTHI:

BTK_15640

BTC:	CT43_CH2820

BTF:	YBT020_14125

BTM:

MC28_2013

BTG:	BTB_c29450(gbpA2)

BTI:

BTG_05205

BTN:	BTF1_11665

BTHT:

H175_ch2869

BTHU:

YBT1518_15585

BTW:	BF38_3995(cbp)

BTHY:

AQ980_15395

BWE:	BcerKBAB4_2627

BWW:	bwei_2205(cbp)

BMYO:

BG05_3199(cbp)

BTY:	Btoyo_0110

BBY:	CY96_12895

BWD:	CT694_15060

BTRO:

FJR70_05035

BMOB:

MLA2C4_14945

BNT:	GSN03_13630

BPAC:

LMD38_12955

BPAN:

NLJ82_13295

BALU:

QRY64_16225

LWI:	UE46_16005

LNW:	OTR81_05500

BLR:	BRLA_c009390

BRW:	GOP56_20670

LFB:	C1X05_10565

KPUL:

GXN76_13300

KEB:	GXN75_09120

LPL:

lp_1697

LPJ:

JDM1_1428

LPT:	zj316_1693

LPS:	LPST_C1354

LPR:	LBP_cg1304

LPZ:

Lp16_1305

LPB:	SH83_07075

LPX:	ASU28_07070

PACI:

A4V11_09585

LSA:

LCA_1008

EFA:

EF0362

EFL:

EF62_0697

EFI:	OG1RF_10251

EFD:	EFD32_0297

EFS:

EFS1_0249

EFN:	DENG_00351(cpbD)

EFQ:	DR75_2356(cbp)

EFC:	EFAU004_01344

EFAU:

EFAU085_00993

EFU:	HMPREF0351_10949

EFM:

M7W_1425

EFT:	M395_06395

EHR:

EHR_14350

EMU:

EMQU_0940

EDU:

LIU_05635

ESS:	ATZ33_10090

ETH:	CK496_07330

ELAC:

I4Q40_09110

ERAF:

J9537_16525

VFV:	K5K99_12265

CML:	BN424_280(chb)

CDJ:	BFC22_11865 BFC22_11870

» show all

Reference

1 [PMID:20929773]

Authors

Vaaje-Kolstad G, Westereng B, Horn SJ, Liu Z, Zhai H, Sorlie M, Eijsink VG

Title

An oxidative enzyme boosting the enzymatic conversion of recalcitrant polysaccharides.

Journal

Science 330:219-22 (2010)
DOI:10.1126/science.1192231

Reference

2 [PMID:22210154]

Authors

Vaaje-Kolstad G, Bohle LA, Gaseidnes S, Dalhus B, Bjoras M, Mathiesen G, Eijsink VG

Title

Characterization of the chitinolytic machinery of Enterococcus faecalis V583 and high-resolution structure of its oxidative CBM33 enzyme.

Journal

J Mol Biol 416:239-54 (2012)
DOI:10.1016/j.jmb.2011.12.033

Sequence

[efa:EF0362]

Reference

3 [PMID:24828494]

Authors

Gudmundsson M, Kim S, Wu M, Ishida T, Momeni MH, Vaaje-Kolstad G, Lundberg D, Royant A, Stahlberg J, Eijsink VG, Beckham GT, Sandgren M

Title

Structural and electronic snapshots during the transition from a Cu(II) to Cu(I) metal center of a lytic polysaccharide monooxygenase by X-ray photoreduction.

Journal

J Biol Chem 289:18782-92 (2014)
DOI:10.1074/jbc.M114.563494

Sequence

[efa:EF0362]

Reference

4 [PMID:25936286]

Authors

Zhang H, Zhao Y, Cao H, Mou G, Yin H

Title

Expression and characterization of a lytic polysaccharide monooxygenase from Bacillus thuringiensis.

Journal

Int J Biol Macromol 79:72-5 (2015)
DOI:10.1016/j.ijbiomac.2015.04.054

Sequence

[btt:HD73_3152]

Other DBs

ExplorEnz - The Enzyme Database:

1.14.99.53

IUBMB Enzyme Nomenclature:

1.14.99.53

ExPASy - ENZYME nomenclature database:

1.14.99.53

BRENDA, the Enzyme Database:

1.14.99.53

All links

Chemical substance (6)   
   KEGG COMPOUND (6)   
Chemical reaction (1)   
   KEGG REACTION (1)   
Gene (95)   
   KEGG ORTHOLOGY (1)   
   KEGG GENES (94)   
Protein sequence (17)   
   UniProt (15)   
   SWISS-PROT (2)   
DNA sequence (39)   
   GenBank (20)   
   EMBL (19)   
Protein domain (3)   
   InterPro (3)   
All databases (161)   

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