Jaffa (also corker) 
an exceptionally well bowled, practically unplayable delivery, usually but not always from a fast bowler. Jayadevans system
an unsuccessful proposal for a rain rule, as an alternative to the Duckworth-Lewis system. Has never been used in professional cricket. Jockstrap (also jock strap)
underwear for male cricketers, designed to securely hold a cricket box in place when batting or wicket keeping. Just not cricket
see its (just) not cricket

K
Keeper
see wicket-keeper

Keep wicket
1. For a wicketkeeper to field. 2. "Keep wickets in hand", which is when a batting team tries to have relatively few of its batters get out. Usually done so that more run-scoring risks can be taken near the end of their innings in a limited-overs match, since they will have many batters left and only a few balls left. King pair
see Golden pair. Knock
a batsmans innings. A batsman who makes a high score in an innings can be said to have had a "good knock". Knuckle ball
A type of delivery where the fast bowler holds the ball on the knuckles of their index and middle finger. A type of slower ball. Kolpak
an overseas player who plays in English domestic cricket under the Kolpak ruling. Kwik cricket
(or quick cricket) An informal version of cricket with sped-up rules, specifically designed to introduce children to the sport. L
Lappa
The Indian version of the hoik. Comes from the English lap, an old term for a stroke somewhere between a pull and a sweep.
The molybdenum centre has a square pyramidal geometry and is distinguished from the xanthine oxidase family by the orientation of the oxo group facing downwards rather than up. Active site and mechanism
The active site of sulfite oxidase contains the molybdopterin cofactor and supports molybdenum in its highest oxidation state, +6 (MoVI). In the enzymes oxidized state, molybdenum is coordinated by a cysteine thiolate, the dithiolene group of molybdopterin, and two terminal oxygen atoms (oxos). Upon reacting with sulfite, one oxygen atom is transferred to sulfite to produce sulfate, and the molybdenum center is reduced by two electrons to MoIV. Water then displaces sulfate, and the removal of two protons (H+) and two electrons (e−) returns the active site to its original state. A key feature of this oxygen atom transfer enzyme is that the oxygen atom being transferred arises from water, not from dioxygen (O2). Electrons are passed one at a time from the molybdenum to the heme group which reacts with cytochrome c to reoxidize the enzyme. The electrons from this reaction enter the electron transport chain (ETC). This reaction is generally the rate limiting reaction. Upon reaction of the enzyme with sulfite, it is reduced by 2 electrons. The negative potential seen with re-reduction of the enzyme shows the oxidized state is favoured. Among the Mo enzyme classes, sulfite oxidase is the most easily oxidized. Although under low pH conditions the oxidative reaction become partially rate limiting. Deficiency
Sulfite oxidase is required to metabolize the sulfur-containing amino acids cysteine and methionine in foods.